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Glutamate receptor ionotropic, kainate 2 (GluK2) (Excitatory amino acid receptor 4) (EAA4) (Glutamate receptor 6) (GluR-6) (GluR6)

 GRIK2_HUMAN             Reviewed;         908 AA.
Q13002; A6NMY9; B5MCV0; D7RWZ3; D7RWZ4; D7RWZ5; D7RWZ6; D7RWZ7;
Q8WWS1; Q96KS6; Q96KS7; Q96KS8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
31-JAN-2018, entry version 177.
RecName: Full=Glutamate receptor ionotropic, kainate 2;
Short=GluK2;
AltName: Full=Excitatory amino acid receptor 4;
Short=EAA4;
AltName: Full=Glutamate receptor 6;
Short=GluR-6;
Short=GluR6;
Flags: Precursor;
Name=GRIK2; Synonyms=GLUR6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=7536611;
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.;
"Functional expression and pharmacological characterization of the
human EAA4 (GluR6) glutamate receptor: a kainate selective channel
subunit.";
Recept. Channels 2:327-337(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8034316; DOI=10.1006/geno.1994.1198;
Paschen W., Blackstone C.D., Huganir R.L., Ross C.A.;
"Human GluR6 kainate receptor (GRIK2): molecular cloning, expression,
polymorphism, and chromosomal assignment.";
Genomics 20:435-440(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Langer A., Xu D., Kuehcke K., Fehse B., Abdallah S., Lother H.;
"Myeloid progenitor cell growth and apoptosis involves know and cell-
specific ionotropic glutamate receptor.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND GENE
ORGANIZATION.
PubMed=11675011; DOI=10.1016/S0378-1119(01)00611-4;
Barbon A., Vallini I., Barlati S.;
"Genomic organization of the human GRIK2 gene and characterization of
multiple splicing variants.";
Gene 274:187-197(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 5; 6 AND 7), AND
ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=20230879; DOI=10.1016/j.gene.2010.03.002;
Zhawar V.K., Kaur G., deRiel J.K., Kaur G.P., Kandpal R.P.,
Athwal R.S.;
"Novel spliced variants of ionotropic glutamate receptor GluR6 in
normal human fibroblast and brain cells are transcribed by tissue
specific promoters.";
Gene 459:1-10(2010).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
RNA EDITING OF POSITION 621.
PubMed=7523595;
Paschen W., Hedreen J.C., Ross C.A.;
"RNA editing of the glutamate receptor subunits GluR2 and GluR6 in
human brain tissue.";
J. Neurochem. 63:1596-1602(1994).
[9]
RNA EDITING OF POSITIONS 567; 571 AND 621.
TISSUE=Brain;
PubMed=7696618;
Nutt S.L., Kamboj R.K.;
"RNA editing of human kainate receptor subunits.";
NeuroReport 5:2625-2629(1994).
[10]
INTERACTION WITH DLG4.
PubMed=11744724; DOI=10.1074/jbc.M109453200;
Piserchio A., Pellegrini M., Mehta S., Blackman S.M., Garcia E.P.,
Marshall J., Mierke D.F.;
"The PDZ1 domain of SAP90. Characterization of structure and
binding.";
J. Biol. Chem. 277:6967-6973(2002).
[11]
PHOSPHORYLATION AT SER-846 AND SER-868, AND SUMOYLATION AT LYS-886.
PubMed=22808340; DOI=10.4161/cib.19195;
Wilkinson K.A., Konopacki F., Henley J.M.;
"Modification and movement: Phosphorylation and SUMOylation regulate
endocytosis of GluK2-containing kainate receptors.";
Commun. Integr. Biol. 5:223-226(2012).
[12]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 429-806 IN COMPLEX WITH
AGONIST.
PubMed=21893069; DOI=10.1016/j.jmb.2011.08.043;
Unno M., Shinohara M., Takayama K., Tanaka H., Teruya K., Doh-ura K.,
Sakai R., Sasaki M., Ikeda-Saito M.;
"Binding and selectivity of the marine toxin neodysiherbaine A and its
synthetic analogues to GluK1 and GluK2 kainate receptors.";
J. Mol. Biol. 413:667-683(2011).
[13]
VARIANT [LARGE SCALE ANALYSIS] GLN-187.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[14]
INVOLVEMENT IN MRT6.
PubMed=17847003; DOI=10.1086/521275;
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.;
"A defect in the ionotropic glutamate receptor 6 gene (GRIK2) is
associated with autosomal recessive mental retardation.";
Am. J. Hum. Genet. 81:792-798(2007).
[15]
VARIANTS THR-657 AND ILE-867, CHARACTERIZATION OF VARIANT THR-657, AND
FUNCTION.
PubMed=28180184; DOI=10.1212/NXG.0000000000000129;
Guzman Y.F., Ramsey K., Stolz J.R., Craig D.W., Huentelman M.J.,
Narayanan V., Swanson G.T.;
"A gain-of-function mutation in the GRIK2 gene causes
neurodevelopmental deficits.";
Neurol. Genet. 3:E129-E129(2017).
-!- FUNCTION: 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 (PubMed:28180184). May be involved in the
transmission of light information from the retina to the
hypothalamus. Modulates cell surface expression of NETO2 (By
similarity). {ECO:0000250|UniProtKB:P39087,
ECO:0000269|PubMed:28180184}.
-!- SUBUNIT: 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). {ECO:0000250, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Cell junction, synapse, postsynaptic cell membrane; Multi-pass
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=A;
IsoId=Q13002-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=Q13002-2; Sequence=VSP_022335;
Name=3;
IsoId=Q13002-3; Sequence=VSP_022337;
Name=4;
IsoId=Q13002-4; Sequence=VSP_022334;
Name=5; Synonyms=C;
IsoId=Q13002-5; Sequence=VSP_022336;
Name=6; Synonyms=D;
IsoId=Q13002-6; Sequence=VSP_044388, VSP_022335;
Note=Seems to be specific for non-neuronal cells. May not
function as active channel.;
Name=7; Synonyms=E;
IsoId=Q13002-7; Sequence=VSP_044389, VSP_022336;
Note=Seems to be specific for non-neuronal cells. May not
function as active channel.;
-!- TISSUE SPECIFICITY: Expression is higher in cerebellum than in
cerebral cortex.
-!- PTM: Sumoylation mediates kainate receptor-mediated endocytosis
and regulates synaptic transmission. Sumoylation is enhanced by
PIAS3 and desumoylated by SENP1 (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. Ubiquitination regulates the GRIK2 levels at
the synapse by leading kainate receptor degradation through
proteasome (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated by PKC at Ser-868 upon agonist activation,
this directly enhance sumoylation. {ECO:0000269|PubMed:22808340}.
-!- RNA EDITING: Modified_positions=567 {ECO:0000269|PubMed:7696618},
571 {ECO:0000269|PubMed:7696618}, 621 {ECO:0000269|PubMed:7523595,
ECO:0000269|PubMed:7696618}; Note=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).;
-!- DISEASE: 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. {ECO:0000269|PubMed:17847003}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- 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.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. GRIK2 subfamily. {ECO:0000305}.
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EMBL; U16126; AAC50420.1; -; mRNA.
EMBL; AJ252246; CAC81020.1; -; mRNA.
EMBL; AJ301608; CAC67485.1; -; mRNA.
EMBL; AJ301609; CAC67486.1; -; mRNA.
EMBL; AJ301610; CAC67487.1; -; mRNA.
EMBL; HM149335; ADH93569.1; -; mRNA.
EMBL; HM149336; ADH93570.1; -; mRNA.
EMBL; HM149337; ADH93571.1; -; mRNA.
EMBL; HM149338; ADH93572.1; -; mRNA.
EMBL; HM149339; ADH93573.1; -; mRNA.
EMBL; AL109919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48448.1; -; Genomic_DNA.
CCDS; CCDS5048.1; -. [Q13002-1]
CCDS; CCDS5049.1; -. [Q13002-2]
CCDS; CCDS55045.1; -. [Q13002-5]
PIR; A54260; A54260.
RefSeq; NP_001159719.1; NM_001166247.1. [Q13002-5]
RefSeq; NP_068775.1; NM_021956.4. [Q13002-1]
RefSeq; NP_786944.1; NM_175768.3. [Q13002-2]
RefSeq; XP_005267002.1; XM_005266945.2. [Q13002-1]
RefSeq; XP_011534079.1; XM_011535777.2. [Q13002-5]
RefSeq; XP_011534080.1; XM_011535778.2. [Q13002-2]
UniGene; Hs.98262; -.
PDB; 3QXM; X-ray; 1.65 A; A/B=429-544, A/B=667-806.
PDB; 5CMM; X-ray; 1.27 A; A=667-806.
PDBsum; 3QXM; -.
PDBsum; 5CMM; -.
ProteinModelPortal; Q13002; -.
SMR; Q13002; -.
BioGrid; 109155; 13.
IntAct; Q13002; 2.
STRING; 9606.ENSP00000397026; -.
BindingDB; Q13002; -.
ChEMBL; CHEMBL3683; -.
DrugBank; DB01351; Amobarbital.
DrugBank; DB01352; Aprobarbital.
DrugBank; DB01483; Barbital.
DrugBank; DB01496; Barbituric acid derivative.
DrugBank; DB00237; Butabarbital.
DrugBank; DB00241; Butalbital.
DrugBank; DB01353; Butethal.
DrugBank; DB02852; Domoic Acid.
DrugBank; DB01354; Heptabarbital.
DrugBank; DB01355; Hexobarbital.
DrugBank; DB00142; L-Glutamic Acid.
DrugBank; DB00463; Metharbital.
DrugBank; DB00849; Methylphenobarbital.
DrugBank; DB00312; Pentobarbital.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB00794; Primidone.
DrugBank; DB02999; Quisqualate.
DrugBank; DB00418; Secobarbital.
DrugBank; DB00306; Talbutal.
DrugBank; DB00599; Thiopental.
GuidetoPHARMACOLOGY; 451; -.
iPTMnet; Q13002; -.
PhosphoSitePlus; Q13002; -.
SwissPalm; Q13002; -.
BioMuta; GRIK2; -.
DMDM; 2492627; -.
MaxQB; Q13002; -.
PaxDb; Q13002; -.
PeptideAtlas; Q13002; -.
PRIDE; Q13002; -.
DNASU; 2898; -.
Ensembl; ENST00000369138; ENSP00000358134; ENSG00000164418. [Q13002-5]
Ensembl; ENST00000413795; ENSP00000405596; ENSG00000164418. [Q13002-2]
Ensembl; ENST00000421544; ENSP00000397026; ENSG00000164418. [Q13002-1]
GeneID; 2898; -.
KEGG; hsa:2898; -.
UCSC; uc003pqo.5; human. [Q13002-1]
CTD; 2898; -.
DisGeNET; 2898; -.
EuPathDB; HostDB:ENSG00000164418.19; -.
GeneCards; GRIK2; -.
H-InvDB; HIX0006094; -.
HGNC; HGNC:4580; GRIK2.
HPA; CAB022463; -.
HPA; HPA014395; -.
HPA; HPA014623; -.
MalaCards; GRIK2; -.
MIM; 138244; gene.
MIM; 611092; phenotype.
neXtProt; NX_Q13002; -.
OpenTargets; ENSG00000164418; -.
Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
PharmGKB; PA164741600; -.
eggNOG; KOG1054; Eukaryota.
eggNOG; ENOG410XPSH; LUCA.
GeneTree; ENSGT00760000118920; -.
HOGENOM; HOG000234371; -.
HOVERGEN; HBG051839; -.
InParanoid; Q13002; -.
KO; K05202; -.
OMA; DSDIQHS; -.
OrthoDB; EOG091G02LN; -.
PhylomeDB; Q13002; -.
TreeFam; TF334668; -.
Reactome; R-HSA-451307; Activation of Na-permeable kainate receptors.
Reactome; R-HSA-451308; Activation of Ca-permeable Kainate Receptor.
SignaLink; Q13002; -.
SIGNOR; Q13002; -.
GeneWiki; GRIK2; -.
GenomeRNAi; 2898; -.
PRO; PR:Q13002; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000164418; -.
CleanEx; HS_GRIK2; -.
ExpressionAtlas; Q13002; baseline and differential.
Genevisible; Q13002; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0032983; C:kainate selective glutamate receptor complex; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; IMP:UniProtKB.
GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:UniProtKB.
GO; GO:0015276; F:ligand-gated ion channel activity; TAS:Reactome.
GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0007215; P:glutamate receptor signaling pathway; TAS:ProtInc.
GO; GO:0060080; P:inhibitory postsynaptic potential; IEA:Ensembl.
GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:UniProtKB.
GO; GO:0043113; P:receptor clustering; IEA:Ensembl.
GO; GO:0046328; P:regulation of JNK cascade; IEA:Ensembl.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:UniProtKB.
GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0006810; P:transport; NAS:ProtInc.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 1.
PRINTS; PR00177; NMDARECEPTOR.
SMART; SM00918; Lig_chan-Glu_bd; 1.
SMART; SM00079; PBPe; 1.
SUPFAM; SSF53822; SSF53822; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Complete proteome; Disease mutation; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Isopeptide bond; Ligand-gated ion channel;
Membrane; Mental retardation; Phosphoprotein; Polymorphism;
Postsynaptic cell membrane; Receptor; Reference proteome; RNA editing;
Signal; Synapse; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 908 Glutamate receptor ionotropic, kainate 2.
/FTId=PRO_0000011544.
TOPO_DOM 32 561 Extracellular. {ECO:0000255}.
TRANSMEM 562 582 Helical. {ECO:0000255}.
TOPO_DOM 583 635 Cytoplasmic. {ECO:0000255}.
TRANSMEM 636 656 Helical. {ECO:0000255}.
TOPO_DOM 657 819 Extracellular. {ECO:0000255}.
TRANSMEM 820 840 Helical. {ECO:0000255}.
TOPO_DOM 841 908 Cytoplasmic. {ECO:0000255}.
REGION 516 518 Glutamate binding. {ECO:0000250}.
REGION 689 690 Glutamate binding. {ECO:0000250}.
BINDING 523 523 Glutamate. {ECO:0000250}.
BINDING 738 738 Glutamate. {ECO:0000250}.
MOD_RES 846 846 Phosphoserine; by PKC.
{ECO:0000269|PubMed:22808340}.
MOD_RES 868 868 Phosphoserine; by PKC.
{ECO:0000269|PubMed:22808340}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 378 378 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 412 412 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 546 546 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 96 347 {ECO:0000250}.
CROSSLNK 886 886 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:22808340}.
VAR_SEQ 509 695 Missing (in isoform 6).
{ECO:0000303|PubMed:20230879}.
/FTId=VSP_044388.
VAR_SEQ 510 714 Missing (in isoform 7).
{ECO:0000303|PubMed:20230879}.
/FTId=VSP_044389.
VAR_SEQ 547 622 Missing (in isoform 4).
{ECO:0000303|PubMed:11675011}.
/FTId=VSP_022334.
VAR_SEQ 585 908 Missing (in isoform 3).
{ECO:0000303|PubMed:11675011}.
/FTId=VSP_022337.
VAR_SEQ 855 908 RSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHT
FNDRRLPGKETMA -> ESSIWLVPPYHPDTV (in
isoform 2 and isoform 6).
{ECO:0000303|PubMed:11675011,
ECO:0000303|PubMed:20230879}.
/FTId=VSP_022335.
VAR_SEQ 856 908 SFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTF
NDRRLPGKETMA -> AKTKLPQDYVFLPILESVSISTVLS
SSPSSSSLSSCS (in isoform 5 and isoform
7). {ECO:0000303|PubMed:20230879,
ECO:0000303|Ref.3}.
/FTId=VSP_022336.
VARIANT 187 187 E -> Q (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035694.
VARIANT 567 567 I -> V (in RNA edited version).
/FTId=VAR_000305.
VARIANT 571 571 Y -> C (in RNA edited version).
/FTId=VAR_000306.
VARIANT 621 621 Q -> R (in RNA edited version).
/FTId=VAR_000307.
VARIANT 657 657 A -> T (probable disease-associated
mutation found in a patient with ataxia,
motor and speech delay and intellectual
disability; gain of function).
{ECO:0000269|PubMed:28180184}.
/FTId=VAR_078426.
VARIANT 766 766 V -> I (in dbSNP:rs3213608).
/FTId=VAR_049186.
VARIANT 867 867 M -> I (in dbSNP:rs2235076).
{ECO:0000269|PubMed:28180184}.
/FTId=VAR_037633.
CONFLICT 20 20 L -> P (in Ref. 3; CAC81020 and 5;
ADH93570/ADH93571/ADH93572/ADH93573).
{ECO:0000305}.
CONFLICT 789 789 G -> S (in Ref. 2). {ECO:0000305}.
STRAND 433 437 {ECO:0000244|PDB:3QXM}.
TURN 441 443 {ECO:0000244|PDB:3QXM}.
STRAND 444 446 {ECO:0000244|PDB:3QXM}.
HELIX 455 458 {ECO:0000244|PDB:3QXM}.
STRAND 459 461 {ECO:0000244|PDB:3QXM}.
HELIX 462 474 {ECO:0000244|PDB:3QXM}.
STRAND 478 482 {ECO:0000244|PDB:3QXM}.
TURN 493 495 {ECO:0000244|PDB:3QXM}.
HELIX 500 506 {ECO:0000244|PDB:3QXM}.
STRAND 511 513 {ECO:0000244|PDB:3QXM}.
HELIX 521 524 {ECO:0000244|PDB:3QXM}.
STRAND 527 529 {ECO:0000244|PDB:3QXM}.
STRAND 533 536 {ECO:0000244|PDB:3QXM}.
STRAND 538 544 {ECO:0000244|PDB:3QXM}.
HELIX 671 675 {ECO:0000244|PDB:3QXM}.
STRAND 678 683 {ECO:0000244|PDB:3QXM}.
HELIX 689 696 {ECO:0000244|PDB:3QXM}.
HELIX 700 711 {ECO:0000244|PDB:3QXM}.
HELIX 713 716 {ECO:0000244|PDB:3QXM}.
STRAND 718 720 {ECO:0000244|PDB:3QXM}.
HELIX 721 730 {ECO:0000244|PDB:3QXM}.
STRAND 731 738 {ECO:0000244|PDB:3QXM}.
HELIX 739 748 {ECO:0000244|PDB:3QXM}.
STRAND 752 757 {ECO:0000244|PDB:3QXM}.
STRAND 762 764 {ECO:0000244|PDB:3QXM}.
STRAND 767 769 {ECO:0000244|PDB:3QXM}.
HELIX 774 787 {ECO:0000244|PDB:3QXM}.
HELIX 790 799 {ECO:0000244|PDB:3QXM}.
SEQUENCE 908 AA; 102583 MW; 5F34630524401E84 CRC64;
MKIIFPILSN PVFRRTVKLL LCLLWIGYSQ GTTHVLRFGG IFEYVESGPM GAEELAFRFA
VNTINRNRTL LPNTTLTYDT QKINLYDSFE ASKKACDQLS LGVAAIFGPS HSSSANAVQS
ICNALGVPHI QTRWKHQVSD NKDSFYVSLY PDFSSLSRAI LDLVQFFKWK TVTVVYDDST
GLIRLQELIK APSRYNLRLK IRQLPADTKD AKPLLKEMKR GKEFHVIFDC SHEMAAGILK
QALAMGMMTE YYHYIFTTLD LFALDVEPYR YSGVNMTGFR ILNTENTQVS SIIEKWSMER
LQAPPKPDSG LLDGFMTTDA ALMYDAVHVV SVAVQQFPQM TVSSLQCNRH KPWRFGTRFM
SLIKEAHWEG LTGRITFNKT NGLRTDFDLD VISLKEEGLE KIGTWDPASG LNMTESQKGK
PANITDSLSN RSLIVTTILE EPYVLFKKSD KPLYGNDRFE GYCIDLLREL STILGFTYEI
RLVEDGKYGA QDDANGQWNG MVRELIDHKA DLAVAPLAIT YVREKVIDFS KPFMTLGISI
LYRKPNGTNP GVFSFLNPLS PDIWMYILLA YLGVSCVLFV IARFSPYEWY NPHPCNPDSD
VVENNFTLLN SFWFGVGALM QQGSELMPKA LSTRIVGGIW WFFTLIIISS YTANLAAFLT
VERMESPIDS ADDLAKQTKI EYGAVEDGAT MTFFKKSKIS TYDKMWAFMS SRRQSVLVKS
NEEGIQRVLT SDYAFLMEST TIEFVTQRNC NLTQIGGLID SKGYGVGTPM GSPYRDKITI
AILQLQEEGK LHMMKEKWWR GNGCPEEESK EASALGVQNI GGIFIVLAAG LVLSVFVAVG
EFLYKSKKNA QLEKRSFCSA MVEELRMSLK CQRRLKHKPQ APVIVKTEEV INMHTFNDRR
LPGKETMA


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