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Glutamate receptor 2 (GluR-2) (AMPA-selective glutamate receptor 2) (GluR-B) (GluR-K2) (Glutamate receptor ionotropic, AMPA 2) (GluA2)

 GRIA2_HUMAN             Reviewed;         883 AA.
P42262; A8MT92; I6L997; Q96FP6;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
10-OCT-2002, sequence version 3.
22-NOV-2017, entry version 187.
RecName: Full=Glutamate receptor 2;
Short=GluR-2;
AltName: Full=AMPA-selective glutamate receptor 2;
AltName: Full=GluR-B;
AltName: Full=GluR-K2;
AltName: Full=Glutamate receptor ionotropic, AMPA 2;
Short=GluA2;
Flags: Precursor;
Name=GRIA2; Synonyms=GLUR2;
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 FLIP), AND VARIANT ARG-607.
TISSUE=Brain;
PubMed=8003671;
Sun W., Ferrer-Montiel A.V., Montal M.;
"Primary structure and functional expression of the AMPA/kainate
receptor subunit 2 from human brain.";
NeuroReport 5:441-444(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS FLOP AND 4), AND
VARIANTS ARG-607 AND ARG-608.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
RNA EDITING OF POSITION 607.
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).
[5]
IDENTIFICATION (ISOFORM 3).
PubMed=14687553; DOI=10.1016/S0896-6273(03)00722-0;
Kolleker A., Zhu J.J., Schupp B.J., Qin Y., Mack V., Borchardt T.,
Koehr G., Malinow R., Seeburg P.H., Osten P.;
"Glutamatergic plasticity by synaptic delivery of GluR-B(long)-
containing AMPA receptors.";
Neuron 40:1199-1212(2003).
[6]
INTERACTION WITH PICK1.
PubMed=15247289; DOI=10.1074/jbc.M404499200;
Dev K.K., Nakanishi S., Henley J.M.;
"The PDZ domain of PICK1 differentially accepts protein kinase C-alpha
and GluR2 as interacting ligands.";
J. Biol. Chem. 279:41393-41397(2004).
[7]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=23739980; DOI=10.1523/JNEUROSCI.2626-12.2013;
Salussolia C.L., Gan Q., Kazi R., Singh P., Allopenna J., Furukawa H.,
Wollmuth L.P.;
"A eukaryotic specific transmembrane segment is required for
tetramerization in AMPA receptors.";
J. Neurosci. 33:9840-9845(2013).
[8]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 25-412, SUBUNIT, DISULFIDE
BOND, AND GLYCOSYLATION AT ASN-370.
PubMed=19651138; DOI=10.1016/j.jmb.2009.07.082;
Clayton A., Siebold C., Gilbert R.J., Sutton G.C., Harlos K.,
McIlhinney R.A., Jones E.Y., Aricescu A.R.;
"Crystal structure of the GluR2 amino-terminal domain provides
insights into the architecture and assembly of ionotropic glutamate
receptors.";
J. Mol. Biol. 392:1125-1132(2009).
[9]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 413-795 IN COMPLEX WITH
GLUTAMATE AND SYNTHETIC INHIBITOR, AND FUNCTION.
PubMed=20614889; DOI=10.1021/jm1005429;
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.;
"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.";
J. Med. Chem. 53:5801-5812(2010).
[10]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 413-796 IN COMPLEX WITH
GLUTAMATE AND SYNTHETIC INHIBITOR, AND DISULFIDE BOND.
PubMed=21531559; DOI=10.1016/j.bmcl.2011.04.017;
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.;
"Quinazolinedione sulfonamides: a novel class of competitive AMPA
receptor antagonists with oral activity.";
Bioorg. Med. Chem. Lett. 21:3358-3361(2011).
-!- FUNCTION: 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. {ECO:0000269|PubMed:20614889}.
-!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
receptor subunits. Tetramers may be formed by the dimerization of
dimers. May interact with MPP4. Forms a ternary complex with GRIP1
and CSPG4. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-
catalyzed ATP hydrolysis disrupts binding to ATAD1 and to GRIP1
and leads to AMPAR complex disassembly. Interacts with GRIP2.
Isoform 1, but not isoform 3, interacts with PICK1/PRKCABP.
Interacts with GRIA1 and SYNDIG1. Interacts with LRFN1 (By
similarity). Found in a complex with GRIA1, GRIA3, GRIA4, CNIH2,
CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8.
Interacts with CACNG5 (By similarity). Interacts with SNX27 (via
PDZ domain); the interaction is required for recycling to the
plasma membrane when endocytosed and prevent degradation in
lysosomes. Interacts with OLFM2 (By similarity). Interacts with
AP4B1, AP4E1 and AP4M1; probably indirect it mediates the
somatodendritic localization of GRIA2 in neurons (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P23819}.
-!- INTERACTION:
P46459:NSF; NbExp=2; IntAct=EBI-3909876, EBI-712251;
Q9EP80:Pick1 (xeno); NbExp=2; IntAct=EBI-3909876, EBI-77728;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23739980};
Multi-pass membrane protein {ECO:0000269|PubMed:23739980}.
Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell
membrane {ECO:0000269|PubMed:23739980}; Multi-pass membrane
protein {ECO:0000269|PubMed:23739980}. Note=Interaction with
CACNG2, CNIH2 and CNIH3 promotes cell surface expression (By
similarity). Displays a somatodendritic localization and is
excluded from axons in neurons (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P23819}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=Flop;
IsoId=P42262-1; Sequence=Displayed;
Name=Flip;
IsoId=P42262-2; Sequence=VSP_053350;
Name=3; Synonyms=Long;
IsoId=P42262-3; Sequence=VSP_029309;
Name=4;
IsoId=P42262-4; Sequence=VSP_055920, VSP_053350;
Note=No experimental confirmation available.;
-!- DOMAIN: The M4 transmembrane segment mediates tetramerization and
is required for cell surface expression.
-!- PTM: 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). {ECO:0000250}.
-!- RNA EDITING: Modified_positions=607 {ECO:0000269|PubMed:7523595};
Note=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.;
-!- 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.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. GRIA2 subfamily. {ECO:0000305}.
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EMBL; L20814; AAA58631.1; -; mRNA.
EMBL; AC079233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC112240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010574; AAH10574.1; -; mRNA.
EMBL; BC028736; AAH28736.2; -; mRNA.
CCDS; CCDS3797.1; -. [P42262-2]
CCDS; CCDS43274.1; -. [P42262-1]
CCDS; CCDS43275.1; -. [P42262-4]
PIR; I58181; I58181.
RefSeq; NP_000817.2; NM_000826.3.
RefSeq; NP_001077088.1; NM_001083619.1.
RefSeq; NP_001077089.1; NM_001083620.1.
RefSeq; XP_016863605.1; XM_017008116.1. [P42262-4]
RefSeq; XP_016863606.1; XM_017008117.1. [P42262-4]
UniGene; Hs.32763; -.
PDB; 2WJW; X-ray; 1.80 A; A=25-412.
PDB; 2WJX; X-ray; 4.10 A; A/B/C=25-412.
PDB; 2XHD; X-ray; 1.80 A; A/B=413-527, A/B=653-796.
PDB; 3R7X; X-ray; 2.10 A; A/B=413-527, A/B=653-796.
PDB; 3RN8; X-ray; 1.70 A; A/B/C=413-527, A/B/C=653-812.
PDB; 3RNN; X-ray; 1.75 A; A/B/C=413-527, A/B/C=653-812.
PDB; 3UA8; X-ray; 1.90 A; A=413-527, A=653-796.
PDB; 5H8S; X-ray; 1.70 A; A/B/C=413-527, A/B/C=653-796.
PDBsum; 2WJW; -.
PDBsum; 2WJX; -.
PDBsum; 2XHD; -.
PDBsum; 3R7X; -.
PDBsum; 3RN8; -.
PDBsum; 3RNN; -.
PDBsum; 3UA8; -.
PDBsum; 5H8S; -.
ProteinModelPortal; P42262; -.
SMR; P42262; -.
BioGrid; 109148; 32.
CORUM; P42262; -.
DIP; DIP-42852N; -.
IntAct; P42262; 15.
MINT; MINT-2791741; -.
STRING; 9606.ENSP00000264426; -.
BindingDB; P42262; -.
ChEMBL; CHEMBL4016; -.
DrugBank; DB02057; (S)-AMPA.
DrugBank; DB03319; (S)-ATPA.
DrugBank; DB01664; (S)-Des-Me-Ampa.
DrugBank; DB02347; 2-Amino-3-(5-Tert-Butyl-3-(Phosphonomethoxy)-4-Isoxazolyl)Propionic Acid.
DrugBank; DB01351; Amobarbital.
DrugBank; DB04599; Aniracetam.
DrugBank; DB01352; Aprobarbital.
DrugBank; DB01483; Barbital.
DrugBank; DB01496; Barbituric acid derivative.
DrugBank; DB04000; Bromo-Willardiine.
DrugBank; DB00237; Butabarbital.
DrugBank; DB00241; Butalbital.
DrugBank; DB01353; Butethal.
DrugBank; DB05047; CX717.
DrugBank; DB00898; Ethanol.
DrugBank; DB03759; FG-9041.
DrugBank; DB02966; Fluoro-Willardiine.
DrugBank; DB01354; Heptabarbital.
DrugBank; DB01355; Hexobarbital.
DrugBank; DB02818; Iodo-Willardiine.
DrugBank; DB00142; L-Glutamic Acid.
DrugBank; DB00463; Metharbital.
DrugBank; DB00849; Methylphenobarbital.
DrugBank; DB00312; Pentobarbital.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB00794; Primidone.
DrugBank; DB01346; Quinidine barbiturate.
DrugBank; DB02999; Quisqualate.
DrugBank; DB00418; Secobarbital.
DrugBank; DB04982; Talampanel.
DrugBank; DB00306; Talbutal.
DrugBank; DB04798; THIO-ATPA.
DrugBank; DB00599; Thiopental.
DrugBank; DB04129; Willardiine.
GuidetoPHARMACOLOGY; 445; -.
TCDB; 1.A.10.1.13; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
iPTMnet; P42262; -.
PhosphoSitePlus; P42262; -.
SwissPalm; P42262; -.
BioMuta; GRIA2; -.
DMDM; 23831146; -.
PaxDb; P42262; -.
PeptideAtlas; P42262; -.
PRIDE; P42262; -.
Ensembl; ENST00000264426; ENSP00000264426; ENSG00000120251. [P42262-1]
Ensembl; ENST00000296526; ENSP00000296526; ENSG00000120251. [P42262-2]
Ensembl; ENST00000393815; ENSP00000377403; ENSG00000120251. [P42262-4]
Ensembl; ENST00000507898; ENSP00000426845; ENSG00000120251. [P42262-4]
GeneID; 2891; -.
KEGG; hsa:2891; -.
UCSC; uc003ipk.5; human. [P42262-1]
CTD; 2891; -.
DisGeNET; 2891; -.
EuPathDB; HostDB:ENSG00000120251.18; -.
GeneCards; GRIA2; -.
HGNC; HGNC:4572; GRIA2.
HPA; CAB006830; -.
HPA; CAB007812; -.
HPA; CAB012981; -.
HPA; HPA008441; -.
MIM; 138247; gene.
neXtProt; NX_P42262; -.
OpenTargets; ENSG00000120251; -.
PharmGKB; PA28967; -.
eggNOG; KOG1054; Eukaryota.
eggNOG; ENOG410XPSH; LUCA.
GeneTree; ENSGT00760000118920; -.
HOGENOM; HOG000234372; -.
HOVERGEN; HBG051839; -.
InParanoid; P42262; -.
KO; K05198; -.
OMA; SQEIWVS; -.
OrthoDB; EOG091G11CB; -.
PhylomeDB; P42262; -.
TreeFam; TF315232; -.
Reactome; R-HSA-399710; Activation of AMPA receptors.
Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
Reactome; R-HSA-438066; Unblocking of NMDA receptor, glutamate binding and activation.
SignaLink; P42262; -.
SIGNOR; P42262; -.
ChiTaRS; GRIA2; human.
EvolutionaryTrace; P42262; -.
GeneWiki; GRIA2; -.
GenomeRNAi; 2891; -.
PRO; PR:P42262; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000120251; -.
CleanEx; HS_GRIA2; -.
ExpressionAtlas; P42262; baseline and differential.
Genevisible; P42262; HS.
GO; GO:0032281; C:AMPA glutamate receptor complex; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; ISS:ARUK-UCL.
GO; GO:0043197; C:dendritic spine; NAS:ARUK-UCL.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0060076; C:excitatory synapse; NAS:ARUK-UCL.
GO; GO:0009897; C:external side of plasma membrane; TAS:ARUK-UCL.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0098794; C:postsynapse; TAS:ARUK-UCL.
GO; GO:0098843; C:postsynaptic endocytic zone; NAS:ARUK-UCL.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0004971; F:AMPA glutamate receptor activity; ISS:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL.
GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; TAS:Reactome.
GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0035249; P:synaptic transmission, glutamatergic; TAS:ARUK-UCL.
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; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism;
Postsynaptic cell membrane; Receptor; Reference proteome; RNA editing;
Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 883 Glutamate receptor 2.
/FTId=PRO_0000011532.
TOPO_DOM 25 543 Extracellular. {ECO:0000250}.
TRANSMEM 544 564 Helical. {ECO:0000250}.
TOPO_DOM 565 591 Cytoplasmic. {ECO:0000250}.
INTRAMEM 592 607 Helical; Pore-forming. {ECO:0000250}.
INTRAMEM 608 610 {ECO:0000250}.
TOPO_DOM 611 616 Cytoplasmic. {ECO:0000250}.
TRANSMEM 617 637 Helical. {ECO:0000250}.
TOPO_DOM 638 812 Extracellular. {ECO:0000250}.
TRANSMEM 813 833 Helical; Name=M4.
TOPO_DOM 834 883 Cytoplasmic. {ECO:0000250}.
REGION 499 501 Glutamate binding.
REGION 675 676 Glutamate binding.
BINDING 471 471 Glutamate. {ECO:0000269|PubMed:20614889,
ECO:0000269|PubMed:21531559}.
BINDING 506 506 Glutamate. {ECO:0000269|PubMed:20614889,
ECO:0000269|PubMed:21531559}.
BINDING 726 726 Glutamate. {ECO:0000269|PubMed:20614889,
ECO:0000269|PubMed:21531559}.
MOD_RES 683 683 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P19491}.
MOD_RES 717 717 Phosphoserine; by PKG.
{ECO:0000250|UniProtKB:P19491}.
MOD_RES 860 860 Phosphoserine.
{ECO:0000250|UniProtKB:P23819}.
MOD_RES 863 863 Phosphoserine.
{ECO:0000250|UniProtKB:P23819}.
MOD_RES 876 876 Phosphotyrosine.
{ECO:0000250|UniProtKB:P23819}.
MOD_RES 880 880 Phosphoserine.
{ECO:0000250|UniProtKB:P23819}.
LIPID 610 610 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 836 836 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19651138}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 78 330
DISULFID 739 794
VAR_SEQ 1 47 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055920.
VAR_SEQ 765 800 NAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD -> T
PVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSG (in
isoform Flip and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8003671}.
/FTId=VSP_053350.
VAR_SEQ 848 883 VAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI -> M
TLNDAMRNKARLSITGSTGENGRVMTPEFPKAVHAVPYVSP
GMGMNVSVTDLS (in isoform 3).
{ECO:0000305}.
/FTId=VSP_029309.
VARIANT 607 607 Q -> R (in RNA edited version;
dbSNP:rs17850674).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8003671}.
/FTId=VAR_000303.
VARIANT 608 608 Q -> R (in dbSNP:rs17850675).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_037055.
CONFLICT 140 140 I -> V (in Ref. 3; AAH10574).
{ECO:0000305}.
CONFLICT 241 241 G -> E (in Ref. 1; AAA58631).
{ECO:0000305}.
CONFLICT 415 415 T -> I (in Ref. 3; AAH28736).
{ECO:0000305}.
CONFLICT 764 764 R -> G (in Ref. 1; AAA58631).
{ECO:0000305}.
STRAND 27 34 {ECO:0000244|PDB:2WJW}.
HELIX 38 51 {ECO:0000244|PDB:2WJW}.
STRAND 58 65 {ECO:0000244|PDB:2WJW}.
HELIX 70 83 {ECO:0000244|PDB:2WJW}.
STRAND 88 90 {ECO:0000244|PDB:2WJW}.
TURN 94 96 {ECO:0000244|PDB:2WJW}.
HELIX 97 107 {ECO:0000244|PDB:2WJW}.
STRAND 111 113 {ECO:0000244|PDB:2WJW}.
STRAND 125 127 {ECO:0000244|PDB:2WJW}.
HELIX 133 142 {ECO:0000244|PDB:2WJW}.
STRAND 147 152 {ECO:0000244|PDB:2WJW}.
HELIX 159 171 {ECO:0000244|PDB:2WJW}.
STRAND 174 179 {ECO:0000244|PDB:2WJW}.
HELIX 188 191 {ECO:0000244|PDB:2WJW}.
HELIX 193 201 {ECO:0000244|PDB:2WJW}.
STRAND 206 211 {ECO:0000244|PDB:2WJW}.
HELIX 213 225 {ECO:0000244|PDB:2WJW}.
HELIX 230 232 {ECO:0000244|PDB:2WJW}.
STRAND 234 237 {ECO:0000244|PDB:2WJW}.
STRAND 239 241 {ECO:0000244|PDB:2WJW}.
HELIX 247 249 {ECO:0000244|PDB:2WJW}.
STRAND 256 262 {ECO:0000244|PDB:2WJW}.
HELIX 268 277 {ECO:0000244|PDB:2WJW}.
TURN 282 284 {ECO:0000244|PDB:2WJW}.
STRAND 289 291 {ECO:0000244|PDB:2WJW}.
HELIX 295 316 {ECO:0000244|PDB:2WJW}.
HELIX 341 349 {ECO:0000244|PDB:2WJW}.
STRAND 353 355 {ECO:0000244|PDB:2WJW}.
STRAND 358 360 {ECO:0000244|PDB:2WJW}.
STRAND 366 368 {ECO:0000244|PDB:2WJW}.
STRAND 373 379 {ECO:0000244|PDB:2WJW}.
STRAND 382 390 {ECO:0000244|PDB:2WJW}.
TURN 391 393 {ECO:0000244|PDB:2WJW}.
STRAND 394 397 {ECO:0000244|PDB:2WJW}.
STRAND 416 420 {ECO:0000244|PDB:3RN8}.
TURN 424 426 {ECO:0000244|PDB:3RN8}.
STRAND 427 429 {ECO:0000244|PDB:3RN8}.
HELIX 433 435 {ECO:0000244|PDB:3RN8}.
HELIX 438 441 {ECO:0000244|PDB:3RN8}.
STRAND 442 444 {ECO:0000244|PDB:3RN8}.
HELIX 445 457 {ECO:0000244|PDB:3RN8}.
STRAND 461 465 {ECO:0000244|PDB:3RN8}.
TURN 476 478 {ECO:0000244|PDB:3RN8}.
HELIX 483 489 {ECO:0000244|PDB:3RN8}.
STRAND 494 496 {ECO:0000244|PDB:3RN8}.
HELIX 504 507 {ECO:0000244|PDB:3RN8}.
STRAND 510 512 {ECO:0000244|PDB:3RN8}.
STRAND 516 519 {ECO:0000244|PDB:3RN8}.
STRAND 521 526 {ECO:0000244|PDB:3RN8}.
HELIX 657 661 {ECO:0000244|PDB:3RN8}.
STRAND 664 671 {ECO:0000244|PDB:3RN8}.
HELIX 675 682 {ECO:0000244|PDB:3RN8}.
HELIX 686 697 {ECO:0000244|PDB:3RN8}.
STRAND 704 706 {ECO:0000244|PDB:3RN8}.
HELIX 707 716 {ECO:0000244|PDB:3RN8}.
TURN 717 719 {ECO:0000244|PDB:3RN8}.
STRAND 720 726 {ECO:0000244|PDB:3RN8}.
HELIX 727 734 {ECO:0000244|PDB:3RN8}.
STRAND 741 745 {ECO:0000244|PDB:3RN8}.
STRAND 751 753 {ECO:0000244|PDB:3RN8}.
STRAND 756 758 {ECO:0000244|PDB:3RN8}.
HELIX 764 776 {ECO:0000244|PDB:3RN8}.
HELIX 779 788 {ECO:0000244|PDB:3RN8}.
TURN 789 791 {ECO:0000244|PDB:3RN8}.
SEQUENCE 883 AA; 98821 MW; 6DAB96C76D1D8448 CRC64;
MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP
HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG
THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV
GNINNDKKDE MYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL
GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT TTIKYTSALT
YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI
KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT
ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI
WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD
PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF
SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL
SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK
YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLRNAVNLA VLKLNEQGLL
DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR
AEAKRMKVAK NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI


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