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Glutamate receptor ionotropic, NMDA 2A (GluN2A) (Glutamate [NMDA] receptor subunit epsilon-1) (N-methyl D-aspartate receptor subtype 2A) (NMDAR2A) (NR2A)

 NMDE1_RAT               Reviewed;        1464 AA.
Q00959; O08948; Q63728;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
25-OCT-2017, entry version 168.
RecName: Full=Glutamate receptor ionotropic, NMDA 2A;
Short=GluN2A {ECO:0000303|PubMed:27618671};
AltName: Full=Glutamate [NMDA] receptor subunit epsilon-1;
AltName: Full=N-methyl D-aspartate receptor subtype 2A;
Short=NMDAR2A {ECO:0000303|PubMed:8428958};
Short=NR2A {ECO:0000303|PubMed:1350383, ECO:0000303|PubMed:9509416};
Flags: Precursor;
Name=Grin2a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=1350383; DOI=10.1126/science.256.5060.1217;
Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H.,
Burnashev N., Sakmann B., Seeburg P.H.;
"Heteromeric NMDA receptors: molecular and functional distinction of
subtypes.";
Science 256:1217-1221(1992).
[2]
SEQUENCE REVISION TO 595 AND 597-598.
Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H.,
Burnashev N., Sakmann B., Seeburg P.H.;
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, FUNCTION, AND SUBCELLULAR
LOCATION.
STRAIN=Sprague-Dawley; TISSUE=Forebrain;
PubMed=8428958;
Ishii T., Moriyoshi K., Sugihara H., Sakurada K., Kadotani H.,
Yokoi M., Akazawa C., Shigemoto R., Mizuno N., Masu M., Nakanishi S.;
"Molecular characterization of the family of the N-methyl-D-aspartate
receptor subunits.";
J. Biol. Chem. 268:2836-2843(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Boulter J.;
"Nucleotide sequence of rat NMDA receptor gene NMDAR2A.";
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH DLG4.
PubMed=7569905; DOI=10.1126/science.7569905;
Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H.;
"Domain interaction between NMDA receptor subunits and the
postsynaptic density protein PSD-95.";
Science 269:1737-1740(1995).
[6]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9509416;
Jin D.H., Jung Y.W., Ko B.H., Moon I.S.;
"Immunoblot analyses on the differential distribution of NR2A and NR2B
subunits in the adult rat brain.";
Mol. Cells 7:749-754(1997).
[7]
INTERACTION WITH AIP1.
PubMed=9694864; DOI=10.1074/jbc.273.33.21105;
Hirao K., Hata Y., Ide N., Takeuchi M., Irie M., Yao I., Deguchi M.,
Toyoda A., Suedhof T.C., Takai Y.;
"A novel multiple PDZ domain-containing molecule interacting with N-
methyl-d-aspartate receptors and neuronal cell adhesion proteins.";
J. Biol. Chem. 273:21105-21110(1998).
[8]
INTERACTION WITH PATJ.
PubMed=9647694; DOI=10.1006/mcne.1998.0679;
Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
"CIPP, a novel multivalent PDZ domain protein, selectively interacts
with Kir4.0 family members, NMDA receptor subunits, neurexins, and
neuroligins.";
Mol. Cell. Neurosci. 11:161-172(1998).
[9]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH GRIN1 AND
GRIN3A.
PubMed=11160393;
Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A.,
Trimmer J.S., Sucher N.J., Heinemann S.F.;
"Assembly with the NR1 subunit is required for surface expression of
NR3A-containing NMDA receptors.";
J. Neurosci. 21:1228-1237(2001).
[10]
IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN3A AND PPP2CB.
PubMed=11588171;
Chan S.F., Sucher N.J.;
"An NMDA receptor signaling complex with protein phosphatase 2A.";
J. Neurosci. 21:7985-7992(2001).
[11]
IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
PubMed=12391275; DOI=10.1124/mol.62.5.1119;
Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B.,
Yasuda R.P.;
"Association of NR3A with the N-methyl-D-aspartate receptor NR1 and
NR2 subunits.";
Mol. Pharmacol. 62:1119-1127(2002).
[12]
IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
PubMed=11929923; DOI=10.1152/jn.00531.2001;
Sasaki Y.F., Rothe T., Premkumar L.S., Das S., Cui J., Talantova M.V.,
Wong H.-K., Gong X., Chan S.F., Zhang D., Nakanishi N., Sucher N.J.,
Lipton S.A.;
"Characterization and comparison of the NR3A subunit of the NMDA
receptor in recombinant systems and primary cortical neurons.";
J. Neurophysiol. 87:2052-2063(2002).
[13]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH GRIN1 AND
GRIN3B.
PubMed=14602821;
Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.;
"Specific assembly with the NMDA receptor 3B subunit controls surface
expression and calcium permeability of NMDA receptors.";
J. Neurosci. 23:10064-10073(2003).
[14]
INTERACTION WITH LRFN2.
PubMed=16495444; DOI=10.1523/JNEUROSCI.3799-05.2006;
Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K.,
Wenthold R.J.;
"A novel family of adhesion-like molecules that interacts with the
NMDA receptor.";
J. Neurosci. 26:2174-2183(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929;
SER-1025; SER-1059; SER-1062; SER-1198 AND SER-1291, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=28384476; DOI=10.1016/j.neuron.2017.03.018;
Sun W., Hansen K.B., Jahr C.E.;
"Allosteric Interactions between NMDA Receptor Subunits Shape the
Developmental Shift in Channel Properties.";
Neuron 94:58-64(2017).
[17] {ECO:0000244|PDB:2A5S, ECO:0000244|PDB:2A5T}
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 402-539 AND 661-802 IN
COMPLEXES WITH GRIN1 AND GLUTAMATE, FUNCTION, SUBCELLULAR LOCATION,
SUBUNIT, DOMAIN, AND DISULFIDE BOND.
PubMed=16281028; DOI=10.1038/nature04089;
Furukawa H., Singh S.K., Mancusso R., Gouaux E.;
"Subunit arrangement and function in NMDA receptors.";
Nature 438:185-192(2005).
[18] {ECO:0000244|PDB:4JWX}
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 402-539 AND 661-802 IN
COMPLEX WITH SYNTHETIC AGONIST, FUNCTION, SUBCELLULAR LOCATION,
SUBUNIT, AND DISULFIDE BONDS.
PubMed=23625947; DOI=10.1124/mol.113.085803;
Hansen K.B., Tajima N., Risgaard R., Perszyk R.E., Jorgensen L.,
Vance K.M., Ogden K.K., Clausen R.P., Furukawa H., Traynelis S.F.;
"Structural determinants of agonist efficacy at the glutamate binding
site of N-methyl-D-aspartate receptors.";
Mol. Pharmacol. 84:114-127(2013).
[19] {ECO:0000244|PDB:4NF4, ECO:0000244|PDB:4NF5, ECO:0000244|PDB:4NF6, ECO:0000244|PDB:4NF8}
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 402-539 AND 661-802 IN
COMPLEXES WITH GRIN1 AND GLUTAMATE, FUNCTION, SUBUNIT, DISULFIDE
BONDS, AND MUTAGENESIS OF PHE-416; TYR-730 AND VAL-734.
PubMed=24462099; DOI=10.1016/j.neuron.2013.11.033;
Jespersen A., Tajima N., Fernandez-Cuervo G., Garnier-Amblard E.C.,
Furukawa H.;
"Structural insights into competitive antagonism in NMDA receptors.";
Neuron 81:366-378(2014).
[20] {ECO:0000244|PDB:5I56, ECO:0000244|PDB:5I57, ECO:0000244|PDB:5I58, ECO:0000244|PDB:5I59, ECO:0000244|PDB:5JTY}
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 402-539 AND 661-800 IN
COMPLEX WITH GRIN1 AND GLUTAMATE, FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, AND DISULFIDE BONDS.
PubMed=27618671; DOI=10.1016/j.neuron.2016.08.014;
Yi F., Mou T.C., Dorsett K.N., Volkmann R.A., Menniti F.S.,
Sprang S.R., Hansen K.B.;
"Structural Basis for Negative Allosteric Modulation of GluN2A-
Containing NMDA Receptors.";
Neuron 91:1316-1329(2016).
[21] {ECO:0000244|PDB:5TPW, ECO:0000244|PDB:5TQ0, ECO:0000244|PDB:5TQ2}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 34-393 IN COMPLEX WITH GRIN1
AND ZINC, FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, SUBUNIT,
MUTAGENESIS OF LYS-233; ASN-264 AND ASP-282, AND DISULFIDE BONDS.
PubMed=27916457; DOI=10.1016/j.neuron.2016.11.006;
Romero-Hernandez A., Simorowski N., Karakas E., Furukawa H.;
"Molecular Basis for Subtype Specificity and High-Affinity Zinc
Inhibition in the GluN1-GluN2A NMDA Receptor Amino-Terminal Domain.";
Neuron 92:1324-1336(2016).
[22] {ECO:0000244|PDB:5U8C}
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 402-539 AND 661-802 IN
COMPLEX WITH GRIN1 AND SYNTHETIC ANTAGONIST, FUNCTION, SUBCELLULAR
LOCATION, SUBUNIT, AND DISULFIDE BONDS.
PubMed=28468946; DOI=10.1124/mol.116.107912;
Romero-Hernandez A., Furukawa H.;
"Novel Mode of Antagonist Binding in NMDA Receptors Revealed by the
Crystal Structure of the GluN1-GluN2A Ligand-Binding Domain Complexed
to NVP-AAM077.";
Mol. Pharmacol. 92:22-29(2017).
[23] {ECO:0000244|PDB:5DEX, ECO:0000244|PDB:5VIH, ECO:0000244|PDB:5VIJ}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 402-539 AND 566-800 IN
COMPLEX WITH GRIN1, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
DISULFIDE BONDS.
PubMed=28760974; DOI=10.1073/pnas.1707752114;
Lind G.E., Mou T.C., Tamborini L., Pomper M.G., De Micheli C.,
Conti P., Pinto A., Hansen K.B.;
"Structural basis of subunit selectivity for competitive NMDA receptor
antagonists with preference for GluN2A over GluN2B subunits.";
Proc. Natl. Acad. Sci. U.S.A. 114:E6942-E6951(2017).
[24] {ECO:0000244|PDB:5VII}
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 402-539 AND 566-800 IN
COMPLEX WITH GRIN1, SUBUNIT, AND DISULFIDE BONDS.
Mou T.C., Sprang S.R., Hansen K.B.;
"Crystal structure of GluN1/GluN2A NMDA receptor agonist binding
domains with glycine and antagonist, phenyl-ACEPC.";
Submitted (APR-2017) to the PDB data bank.
-!- FUNCTION: Component of NMDA receptor complexes that function as
heterotetrameric, ligand-gated ion channels with high calcium
permeability and voltage-dependent sensitivity to magnesium.
Channel activation requires binding of the neurotransmitter
glutamate to the epsilon subunit, glycine binding to the zeta
subunit, plus membrane depolarization to eliminate channel
inhibition by Mg(2+). Sensitivity to glutamate and channel
kinetics depend on the subunit composition; channels containing
GRIN1 and GRIN2A have higher sensitivity to glutamate and faster
kinetics than channels formed by GRIN1 and GRIN2B
(PubMed:28384476). Contributes to the slow phase of excitatory
postsynaptic current, long-term synaptic potentiation, and
learning (By similarity). {ECO:0000250|UniProtKB:P35436,
ECO:0000269|PubMed:1350383, ECO:0000269|PubMed:16281028,
ECO:0000269|PubMed:23625947, ECO:0000269|PubMed:24462099,
ECO:0000269|PubMed:27618671, ECO:0000269|PubMed:27916457,
ECO:0000269|PubMed:28384476, ECO:0000269|PubMed:28468946,
ECO:0000269|PubMed:28760974, ECO:0000269|PubMed:8428958}.
-!- ENZYME REGULATION: Channel activity is inhibited by nM
concentrations of Zn(2+). {ECO:0000269|PubMed:27916457}.
-!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed
of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A,
GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:1350383,
PubMed:8428958, PubMed:28384476, PubMed:16281028, PubMed:23625947,
PubMed:24462099, PubMed:27618671, PubMed:27916457,
PubMed:28468946, PubMed:28760974, Ref.24). Can also form
heterotetrameric channels that contain at least one zeta subunit
(GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B
(PubMed:11160393, PubMed:11588171, PubMed:12391275,
PubMed:11929923). In vivo, the subunit composition may depend on
the expression levels of the different subunits (Probable). Found
in a complex with GRIN1, GRIN3A and PPP2CB (PubMed:11588171).
Found in a complex with GRIN1 and GRIN3B (PubMed:14602821).
Interacts with AIP1 (PubMed:9694864). Interacts with HIP1 and
NETO1. Interacts with SNX27 (via PDZ domain); the interaction is
required for recycling to the plasma membrane when endocytosed and
prevent degradation in lysosomes (By similarity). Interacts with
PDZ domains of PATJ and DLG4 (PubMed:7569905, PubMed:9647694).
Interacts with LRFN2 (PubMed:16495444).
{ECO:0000250|UniProtKB:P35436, ECO:0000269|PubMed:11160393,
ECO:0000269|PubMed:11588171, ECO:0000269|PubMed:11929923,
ECO:0000269|PubMed:12391275, ECO:0000269|PubMed:1350383,
ECO:0000269|PubMed:14602821, ECO:0000269|PubMed:16281028,
ECO:0000269|PubMed:16495444, ECO:0000269|PubMed:23625947,
ECO:0000269|PubMed:24462099, ECO:0000269|PubMed:27618671,
ECO:0000269|PubMed:27916457, ECO:0000269|PubMed:28384476,
ECO:0000269|PubMed:28468946, ECO:0000269|PubMed:28760974,
ECO:0000269|PubMed:7569905, ECO:0000269|PubMed:8428958,
ECO:0000269|PubMed:9647694, ECO:0000269|PubMed:9694864,
ECO:0000269|Ref.24, ECO:0000305}.
-!- INTERACTION:
P31016:Dlg4; NbExp=5; IntAct=EBI-630970, EBI-375655;
Q8R4I7:Neto1 (xeno); NbExp=4; IntAct=EBI-630970, EBI-2314926;
P05480:Src (xeno); NbExp=5; IntAct=EBI-630970, EBI-298680;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11160393,
ECO:0000269|PubMed:1350383, ECO:0000269|PubMed:14602821,
ECO:0000269|PubMed:16281028, ECO:0000269|PubMed:23625947,
ECO:0000269|PubMed:24462099, ECO:0000269|PubMed:27618671,
ECO:0000269|PubMed:27916457, ECO:0000269|PubMed:28384476,
ECO:0000269|PubMed:28468946, ECO:0000269|PubMed:28760974,
ECO:0000269|PubMed:8428958}; Multi-pass membrane protein
{ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane
{ECO:0000269|PubMed:9509416}; Multi-pass membrane protein
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Detected in brain cortex, olfactory bulb,
hippocampus, striatum, thalamus, superior colliculus, inferior
colliculus, midbrain and cerebellum (at protein level)
(PubMed:9509416). Detected in brain cortex, hypothalamus and
cerebellum. {ECO:0000269|PubMed:1350383,
ECO:0000269|PubMed:9509416}.
-!- DOMAIN: Contains an N-terminal domain, a ligand-binding domain and
a transmembrane domain. Agonist binding to the extracellular
ligand-binding domains triggers channel gating.
{ECO:0000305|PubMed:16281028}.
-!- DOMAIN: A hydrophobic region that gives rise to the prediction of
a transmembrane span does not cross the membrane, but is part of a
discontinuously helical region that dips into the membrane and is
probably part of the pore and of the selectivity filter.
{ECO:0000250|UniProtKB:B7ZSK1}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR2A/GRIN2A subfamily. {ECO:0000305}.
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EMBL; M91561; AAC03565.1; -; mRNA.
EMBL; D13211; BAA02498.1; -; mRNA.
EMBL; AF001423; AAB58801.1; -; mRNA.
PIR; A43274; A43274.
RefSeq; NP_036705.3; NM_012573.3.
UniGene; Rn.9710; -.
PDB; 2A5S; X-ray; 1.70 A; A=401-539.
PDB; 2A5T; X-ray; 2.00 A; B=401-539.
PDB; 4JWX; X-ray; 1.50 A; A=404-539, A=661-802.
PDB; 4NF4; X-ray; 2.00 A; B=402-539, B=661-802.
PDB; 4NF5; X-ray; 1.90 A; B=402-539, B=661-802.
PDB; 4NF6; X-ray; 2.10 A; B=402-539, B=661-802.
PDB; 4NF8; X-ray; 1.86 A; B=402-539, B=661-802.
PDB; 5DEX; X-ray; 2.40 A; B=402-539, B=661-802.
PDB; 5I56; X-ray; 2.28 A; B=402-539, B=661-800.
PDB; 5I57; X-ray; 1.70 A; B=402-539, B=661-800.
PDB; 5I58; X-ray; 2.52 A; B=402-539, B=661-800.
PDB; 5I59; X-ray; 2.25 A; B=402-539, B=661-800.
PDB; 5JTY; X-ray; 2.72 A; B=402-539, B=661-800.
PDB; 5TPW; X-ray; 2.91 A; B=34-393.
PDB; 5TQ0; X-ray; 2.70 A; B=34-393.
PDB; 5TQ2; X-ray; 3.29 A; B=34-393.
PDB; 5U8C; X-ray; 1.60 A; B=402-539, A=661-802.
PDB; 5VIH; X-ray; 2.40 A; B=402-539, B=566-800.
PDB; 5VII; X-ray; 1.95 A; B=402-539, B=566-800.
PDB; 5VIJ; X-ray; 2.10 A; B=402-539, B=566-800.
PDBsum; 2A5S; -.
PDBsum; 2A5T; -.
PDBsum; 4JWX; -.
PDBsum; 4NF4; -.
PDBsum; 4NF5; -.
PDBsum; 4NF6; -.
PDBsum; 4NF8; -.
PDBsum; 5DEX; -.
PDBsum; 5I56; -.
PDBsum; 5I57; -.
PDBsum; 5I58; -.
PDBsum; 5I59; -.
PDBsum; 5JTY; -.
PDBsum; 5TPW; -.
PDBsum; 5TQ0; -.
PDBsum; 5TQ2; -.
PDBsum; 5U8C; -.
PDBsum; 5VIH; -.
PDBsum; 5VII; -.
PDBsum; 5VIJ; -.
ProteinModelPortal; Q00959; -.
SMR; Q00959; -.
BioGrid; 246574; 7.
CORUM; Q00959; -.
DIP; DIP-34031N; -.
IntAct; Q00959; 7.
MINT; MINT-93314; -.
STRING; 10116.ENSRNOP00000042235; -.
BindingDB; Q00959; -.
ChEMBL; CHEMBL310; -.
TCDB; 1.A.10.1.6; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
iPTMnet; Q00959; -.
PhosphoSitePlus; Q00959; -.
SwissPalm; Q00959; -.
UniCarbKB; Q00959; -.
PaxDb; Q00959; -.
PRIDE; Q00959; -.
GeneID; 24409; -.
KEGG; rno:24409; -.
UCSC; RGD:2737; rat.
CTD; 2903; -.
RGD; 2737; Grin2a.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
HOGENOM; HOG000113802; -.
HOVERGEN; HBG052635; -.
InParanoid; Q00959; -.
KO; K05209; -.
PhylomeDB; Q00959; -.
Reactome; R-RNO-6794361; Neurexins and neuroligins.
EvolutionaryTrace; Q00959; -.
PRO; PR:Q00959; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0043197; C:dendritic spine; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
GO; GO:0045202; C:synapse; TAS:UniProtKB.
GO; GO:0043195; C:terminal bouton; IDA:RGD.
GO; GO:0051117; F:ATPase binding; IPI:RGD.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0016595; F:glutamate binding; IDA:RGD.
GO; GO:0035254; F:glutamate receptor binding; IPI:RGD.
GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
GO; GO:0042165; F:neurotransmitter binding; IDA:RGD.
GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0046983; F:protein dimerization activity; IDA:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0005102; F:receptor binding; IPI:RGD.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0022843; F:voltage-gated cation channel activity; IMP:RGD.
GO; GO:0008270; F:zinc ion binding; IDA:RGD.
GO; GO:0001508; P:action potential; IMP:RGD.
GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:RGD.
GO; GO:0071359; P:cellular response to dsRNA; IEP:RGD.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
GO; GO:0071396; P:cellular response to lipid; IEP:RGD.
GO; GO:0071286; P:cellular response to magnesium ion; IEP:RGD.
GO; GO:0071287; P:cellular response to manganese ion; IEP:RGD.
GO; GO:0071294; P:cellular response to zinc ion; IMP:RGD.
GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:RGD.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:RGD.
GO; GO:0007613; P:memory; IDA:UniProtKB.
GO; GO:0010942; P:positive regulation of cell death; IDA:RGD.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:BHF-UCL.
GO; GO:0051262; P:protein tetramerization; IDA:RGD.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:RGD.
GO; GO:0014075; P:response to amine; IEP:RGD.
GO; GO:0060359; P:response to ammonium ion; IEP:RGD.
GO; GO:0051592; P:response to calcium ion; IEP:RGD.
GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0060992; P:response to fungicide; IEP:RGD.
GO; GO:0009416; P:response to light stimulus; IEP:RGD.
GO; GO:0010042; P:response to manganese ion; IEP:RGD.
GO; GO:0051597; P:response to methylmercury; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0051707; P:response to other organism; IEP:RGD.
GO; GO:0048511; P:rhythmic process; IDA:RGD.
GO; GO:0021510; P:spinal cord development; IEP:RGD.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR018884; NMDAR2_C.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 1.
Pfam; PF10565; NMDAR2_C; 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; Calcium; Cell junction; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Ion channel;
Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
Metal-binding; Phosphoprotein; Postsynaptic cell membrane; Receptor;
Reference proteome; Signal; Synapse; Transmembrane;
Transmembrane helix; Transport; Zinc.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 1464 Glutamate receptor ionotropic, NMDA 2A.
/FTId=PRO_0000011576.
TOPO_DOM 23 555 Extracellular. {ECO:0000305}.
TRANSMEM 556 576 Helical. {ECO:0000250|UniProtKB:B7ZSK1}.
TOPO_DOM 577 600 Cytoplasmic. {ECO:0000305}.
INTRAMEM 601 620 Discontinuously helical.
{ECO:0000250|UniProtKB:B7ZSK1}.
TOPO_DOM 621 625 Cytoplasmic. {ECO:0000305}.
TRANSMEM 626 645 Helical. {ECO:0000250|UniProtKB:B7ZSK1}.
TOPO_DOM 646 816 Extracellular. {ECO:0000305}.
TRANSMEM 817 837 Helical. {ECO:0000250|UniProtKB:B7ZSK1}.
TOPO_DOM 838 1464 Cytoplasmic. {ECO:0000305}.
REGION 511 513 Glutamate binding. {ECO:0000244|PDB:2A5S,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4NF4,
ECO:0000244|PDB:4NF8,
ECO:0000244|PDB:5I56,
ECO:0000244|PDB:5I57,
ECO:0000244|PDB:5I58,
ECO:0000244|PDB:5I59,
ECO:0000244|PDB:5JTY,
ECO:0000269|PubMed:16281028}.
REGION 599 620 Pore-forming.
{ECO:0000250|UniProtKB:B7ZSK1}.
REGION 689 690 Glutamate binding. {ECO:0000244|PDB:2A5S,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4NF4,
ECO:0000244|PDB:4NF8,
ECO:0000269|PubMed:16281028,
ECO:0000269|PubMed:24462099}.
REGION 730 731 Glutamate binding. {ECO:0000244|PDB:2A5S,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4NF4,
ECO:0000244|PDB:4NF8,
ECO:0000269|PubMed:16281028,
ECO:0000269|PubMed:24462099}.
MOTIF 1462 1464 PDZ-binding. {ECO:0000305}.
METAL 44 44 Zinc; via tele nitrogen.
{ECO:0000244|PDB:5TPW,
ECO:0000269|PubMed:27916457}.
METAL 128 128 Zinc; via tele nitrogen.
{ECO:0000244|PDB:5TPW,
ECO:0000269|PubMed:27916457}.
METAL 266 266 Zinc. {ECO:0000244|PDB:5TPW,
ECO:0000269|PubMed:27916457}.
METAL 282 282 Zinc. {ECO:0000244|PDB:5TPW,
ECO:0000269|PubMed:27916457}.
BINDING 518 518 Glutamate. {ECO:0000244|PDB:2A5S,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4NF4,
ECO:0000244|PDB:4NF8,
ECO:0000244|PDB:5I56,
ECO:0000244|PDB:5I57,
ECO:0000244|PDB:5I58,
ECO:0000244|PDB:5I59,
ECO:0000244|PDB:5JTY,
ECO:0000269|PubMed:16281028,
ECO:0000269|PubMed:24462099,
ECO:0000269|PubMed:27618671}.
SITE 614 614 Functional determinant of NMDA receptors.
{ECO:0000250}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 929 929 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1025 1025 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1059 1059 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1062 1062 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1198 1198 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1291 1291 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 443 443 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 541 541 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 87 320 {ECO:0000244|PDB:5TPW,
ECO:0000244|PDB:5TQ0,
ECO:0000244|PDB:5TQ2,
ECO:0000269|PubMed:27916457}.
DISULFID 429 455 {ECO:0000244|PDB:2A5S,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4JWX,
ECO:0000244|PDB:4NF4,
ECO:0000244|PDB:4NF5,
ECO:0000244|PDB:4NF6,
ECO:0000244|PDB:4NF8,
ECO:0000244|PDB:5DEX,
ECO:0000244|PDB:5I56,
ECO:0000244|PDB:5I57,
ECO:0000244|PDB:5I58,
ECO:0000244|PDB:5I59,
ECO:0000244|PDB:5JTY,
ECO:0000244|PDB:5U8C,
ECO:0000244|PDB:5VIH,
ECO:0000244|PDB:5VII,
ECO:0000244|PDB:5VIJ,
ECO:0000269|PubMed:16281028,
ECO:0000269|PubMed:24462099,
ECO:0000269|PubMed:27618671,
ECO:0000269|PubMed:28468946,
ECO:0000269|PubMed:28760974,
ECO:0000269|Ref.24}.
DISULFID 436 456 {ECO:0000244|PDB:2A5S,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4JWX,
ECO:0000244|PDB:4NF4,
ECO:0000244|PDB:4NF5,
ECO:0000244|PDB:4NF6,
ECO:0000244|PDB:4NF8,
ECO:0000244|PDB:5DEX,
ECO:0000244|PDB:5I56,
ECO:0000244|PDB:5I57,
ECO:0000244|PDB:5I58,
ECO:0000244|PDB:5I59,
ECO:0000244|PDB:5JTY,
ECO:0000244|PDB:5U8C,
ECO:0000244|PDB:5VIH,
ECO:0000244|PDB:5VII,
ECO:0000244|PDB:5VIJ,
ECO:0000269|PubMed:16281028,
ECO:0000269|PubMed:23625947,
ECO:0000269|PubMed:24462099,
ECO:0000269|PubMed:27618671,
ECO:0000269|PubMed:28468946,
ECO:0000269|PubMed:28760974}.
DISULFID 745 800 {ECO:0000244|PDB:2A5S,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4JWX,
ECO:0000244|PDB:4NF4,
ECO:0000244|PDB:4NF5,
ECO:0000244|PDB:4NF6,
ECO:0000244|PDB:4NF8,
ECO:0000244|PDB:5U8C,
ECO:0000269|PubMed:16281028,
ECO:0000269|PubMed:23625947,
ECO:0000269|PubMed:24462099,
ECO:0000269|PubMed:28468946}.
MUTAGEN 233 233 K->A,R: Nearly abolishes inhibition by
Zn(2+). {ECO:0000269|PubMed:27916457}.
MUTAGEN 264 264 N->W: Nearly abolishes inhibition by
Zn(2+). {ECO:0000269|PubMed:27916457}.
MUTAGEN 282 282 D->A,H: Nearly abolishes inhibition by
Zn(2+). {ECO:0000269|PubMed:27916457}.
MUTAGEN 416 416 F->A: Decreased sensitivity to glutamate.
{ECO:0000269|PubMed:24462099}.
MUTAGEN 730 730 Y->F,L,M: Strongly decreased sensitivity
to glutamate.
{ECO:0000269|PubMed:24462099}.
MUTAGEN 734 734 V->A: Decreased sensitivity to glutamate.
{ECO:0000269|PubMed:24462099}.
CONFLICT 246 246 L -> F (in Ref. 3; BAA02498).
{ECO:0000305}.
CONFLICT 758 758 S -> T (in Ref. 3; BAA02498 and 4;
AAB58801). {ECO:0000305}.
CONFLICT 990 990 E -> D (in Ref. 4; AAB58801).
{ECO:0000305}.
STRAND 35 40 {ECO:0000244|PDB:5TQ0}.
STRAND 42 44 {ECO:0000244|PDB:5TQ0}.
STRAND 68 73 {ECO:0000244|PDB:5TQ0}.
HELIX 79 91 {ECO:0000244|PDB:5TQ0}.
STRAND 96 101 {ECO:0000244|PDB:5TQ0}.
HELIX 108 120 {ECO:0000244|PDB:5TQ0}.
STRAND 124 128 {ECO:0000244|PDB:5TQ0}.
HELIX 129 132 {ECO:0000244|PDB:5TQ0}.
STRAND 144 147 {ECO:0000244|PDB:5TQ0}.
HELIX 151 164 {ECO:0000244|PDB:5TQ0}.
STRAND 169 177 {ECO:0000244|PDB:5TQ0}.
HELIX 180 193 {ECO:0000244|PDB:5TQ0}.
STRAND 194 196 {ECO:0000244|PDB:5TQ0}.
STRAND 198 200 {ECO:0000244|PDB:5TPW}.
STRAND 204 207 {ECO:0000244|PDB:5TQ0}.
HELIX 213 219 {ECO:0000244|PDB:5TQ0}.
STRAND 225 230 {ECO:0000244|PDB:5TQ0}.
HELIX 233 245 {ECO:0000244|PDB:5TQ0}.
TURN 247 249 {ECO:0000244|PDB:5TQ2}.
STRAND 253 257 {ECO:0000244|PDB:5TQ0}.
HELIX 259 262 {ECO:0000244|PDB:5TQ0}.
STRAND 277 281 {ECO:0000244|PDB:5TQ0}.
STRAND 284 286 {ECO:0000244|PDB:5TQ0}.
HELIX 288 309 {ECO:0000244|PDB:5TQ0}.
STRAND 310 312 {ECO:0000244|PDB:5TQ0}.
TURN 335 337 {ECO:0000244|PDB:5TQ0}.
STRAND 338 340 {ECO:0000244|PDB:5TQ0}.
STRAND 341 343 {ECO:0000244|PDB:5TQ2}.
STRAND 346 348 {ECO:0000244|PDB:5TQ2}.
STRAND 354 358 {ECO:0000244|PDB:5TQ0}.
STRAND 362 366 {ECO:0000244|PDB:5TQ0}.
TURN 368 370 {ECO:0000244|PDB:5TPW}.
STRAND 372 377 {ECO:0000244|PDB:5TQ0}.
TURN 379 382 {ECO:0000244|PDB:5TQ0}.
STRAND 406 410 {ECO:0000244|PDB:4JWX}.
TURN 414 416 {ECO:0000244|PDB:4JWX}.
STRAND 417 421 {ECO:0000244|PDB:4JWX}.
TURN 424 426 {ECO:0000244|PDB:4JWX}.
STRAND 434 447 {ECO:0000244|PDB:4JWX}.
STRAND 449 458 {ECO:0000244|PDB:4JWX}.
HELIX 459 471 {ECO:0000244|PDB:4JWX}.
STRAND 475 479 {ECO:0000244|PDB:4JWX}.
STRAND 482 485 {ECO:0000244|PDB:4JWX}.
STRAND 488 491 {ECO:0000244|PDB:5I58}.
HELIX 495 501 {ECO:0000244|PDB:4JWX}.
STRAND 506 508 {ECO:0000244|PDB:4JWX}.
HELIX 516 519 {ECO:0000244|PDB:4JWX}.
STRAND 522 524 {ECO:0000244|PDB:4JWX}.
STRAND 529 531 {ECO:0000244|PDB:4JWX}.
STRAND 533 538 {ECO:0000244|PDB:4JWX}.
HELIX 668 671 {ECO:0000244|PDB:4JWX}.
HELIX 673 675 {ECO:0000244|PDB:4JWX}.
STRAND 676 678 {ECO:0000244|PDB:4JWX}.
STRAND 686 688 {ECO:0000244|PDB:5I59}.
HELIX 689 697 {ECO:0000244|PDB:4JWX}.
HELIX 699 705 {ECO:0000244|PDB:4JWX}.
HELIX 706 708 {ECO:0000244|PDB:4JWX}.
HELIX 713 721 {ECO:0000244|PDB:4JWX}.
STRAND 726 731 {ECO:0000244|PDB:4JWX}.
HELIX 732 740 {ECO:0000244|PDB:4JWX}.
HELIX 743 745 {ECO:0000244|PDB:4JWX}.
STRAND 747 751 {ECO:0000244|PDB:4JWX}.
HELIX 752 754 {ECO:0000244|PDB:4NF5}.
HELIX 755 757 {ECO:0000244|PDB:4JWX}.
STRAND 759 761 {ECO:0000244|PDB:4JWX}.
STRAND 764 766 {ECO:0000244|PDB:4JWX}.
HELIX 772 784 {ECO:0000244|PDB:4JWX}.
HELIX 787 795 {ECO:0000244|PDB:4JWX}.
SEQUENCE 1464 AA; 165469 MW; DC1528E1898DECA4 CRC64;
MGRLGYWTLL VLPALLVWRD PAQNAAAEKG PPALNIAVLL GHSHDVTERE LRNLWGPEQA
TGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF GDDTDQEAVA QMLDFISSQT
FIPILGIHGG ASMIMADKDP TSTFFQFGAS IQQQATVMLK IMQDYDWHVF SLVTTIFPGY
RDFISFIKTT VDNSFVGWDM QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL
SEARSLGLTG YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGLGILT
TAASSMLEKF SYIPEAKASC YGQAEKPETP LHTLHQFMVN VTWDGKDLSF TEEGYQVHPR
LVVIVLNKDR EWEKVGKWEN QTLSLRHAVW PRYKSFSDCE PDDNHLSIVT LEEAPFVIVE
DIDPLTETCV RNTVPCRKFV KINNSTNEGM NVKKCCKGFC IDILKKLSRT VKFTYDLYLV
TNGKHGKKVN NVWNGMIGEV VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS
NGTVSPSAFL EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT
IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA AFMIQEEFVD
QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY MHQYMTRFNQ RGVEDALVSL
KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI GSGYIFASTG YGIALQKGSP WKRQIDLALL
QFVGDGEMEE LETLWLTGIC HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL
FYWKLRFCFT GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS
AKNISNMSNM NSSRMDSPKR ATDFIQRGSL IVDMVSDKGN LIYSDNRSFQ GKDSIFGDNM
NELQTFVANR HKDNLSNYVF QGQHPLTLNE SNPNTVEVAV STESKGNSRP RQLWKKSMES
LRQDSLNQNP VSQRDEKTAE NRTHSLKSPR YLPEEVAHSD ISETSSRATC HREPDNNKNH
KTKDNFKRSM ASKYPKDCSD VDRTYMKTKA SSPRDKIYTI DGEKEPSFHL DPPQFVENIT
LPENVGFPDT YQDHNENFRK GDSTLPMNRN PLHNEDGLPN NDQYKLYAKH FTLKDKGSPH
SEGSDRYRQN STHCRSCLSN LPTYSGHFTM RSPFKCDACL RMGNLYDIDE DQMLQETGNP
ATREEVYQQD WSQNNALQFQ KNKLRINRQH SYDNILDKPR EIDLSRPSRS ISLKDRERLL
EGNLYGSLFS VPSSKLLGNK SSLFPQGLED SKRSKSLLPD HASDNPFLHT YGDDQRLVIG
RCPSDPYKHS LPSQAVNDSY LRSSLRSTAS YCSRDSRGHS DVYISEHVMP YAANKNTMYS
TPRVLNSCSN RRVYKKMPSI ESDV


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