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Glutamate receptor ionotropic, NMDA 2B (GluN2B) (Glutamate [NMDA] receptor subunit epsilon-2) (N-methyl D-aspartate receptor subtype 2B) (NMDAR2B) (NR2B) (N-methyl-D-aspartate receptor subunit 3) (NR3) (hNR3)

 NMDE2_HUMAN             Reviewed;        1484 AA.
Q13224; Q12919; Q13220; Q13225; Q14CU4; Q9UM56;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
20-JUN-2001, sequence version 3.
23-MAY-2018, entry version 187.
RecName: Full=Glutamate receptor ionotropic, NMDA 2B;
Short=GluN2B;
AltName: Full=Glutamate [NMDA] receptor subunit epsilon-2;
AltName: Full=N-methyl D-aspartate receptor subtype 2B;
Short=NMDAR2B {ECO:0000303|PubMed:7959773};
Short=NR2B;
AltName: Full=N-methyl-D-aspartate receptor subunit 3;
Short=NR3;
Short=hNR3 {ECO:0000303|PubMed:7999784};
Flags: Precursor;
Name=GRIN2B; Synonyms=NMDAR2B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-407.
TISSUE=Fetal brain;
PubMed=7999784; DOI=10.1016/0167-4781(94)00189-A;
Adams S.L., Foldes R.L., Kamboj R.K.;
"Human N-methyl-D-aspartate receptor modulatory subunit hNR3: cloning
and sequencing of the cDNA and primary structure of the protein.";
Biochim. Biophys. Acta 1260:105-108(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
SUBUNIT.
TISSUE=Fetal brain;
PubMed=8768735;
Hess S.D., Daggett L.P., Crona J., Deal C., Lu C.-C., Urrutia A.,
Chavez-Noriega L., Ellis S.B., Johnson E.C., Velicelebi G.;
"Cloning and functional characterization of human heteromeric N-
methyl-D-aspartate receptors.";
J. Pharmacol. Exp. Ther. 278:808-816(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Mandich P., Schito A.M., Pizzuti A., Ratti A.;
"Cloning of GRIN2B human subunit.";
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-294 AND 661-1089.
PubMed=7959773; DOI=10.1006/geno.1994.1366;
Mandich P., Schito A.M., Bellone E., Antonacci R., Finelli P.,
Rocchi M., Ajmar F.;
"Mapping of the human NMDAR2B receptor subunit gene (GRIN2B) to
chromosome 12p12.";
Genomics 22:216-218(1994).
[6]
TISSUE SPECIFICITY.
PubMed=9547169; DOI=10.1016/S0304-3940(97)00853-7;
Schito A.M., Pizzuti A., Di Maria E., Schenone A., Ratti A.,
Defferrari R., Bellone E., Mancardi G.L., Ajmar F., Mandich P.;
"mRNA distribution in adult human brain of GRIN2B, a N-methyl-D-
aspartate (NMDA) receptor subunit.";
Neurosci. Lett. 239:49-53(1997).
[7]
INTERACTION WITH MAGI3.
PubMed=10748157; DOI=10.1074/jbc.M909741199;
Wu Y., Dowbenko D., Spencer S., Laura R., Lee J., Gu Q., Lasky L.A.;
"Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of
MAGI3, a novel membrane-associated guanylate kinase.";
J. Biol. Chem. 275:21477-21485(2000).
[8]
IDENTIFICATION IN A COMPLEX WITH GRIN1 AND PRR7, AND INTERACTION WITH
PRR7.
PubMed=27458189; DOI=10.15252/embj.201593070;
Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S.,
Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.;
"Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and
regulates NMDA-mediated excitotoxicity.";
EMBO J. 35:1923-1934(2016).
[9]
CHROMOSOMAL TRANSLOCATIONS, VARIANT MRD6 CYS-682, AND CHARACTERIZATION
OF VARIANT MRD6 CYS-682.
PubMed=20890276; DOI=10.1038/ng.677;
Endele S., Rosenberger G., Geider K., Popp B., Tamer C., Stefanova I.,
Milh M., Kortum F., Fritsch A., Pientka F.K., Hellenbroich Y.,
Kalscheuer V.M., Kohlhase J., Moog U., Rappold G., Rauch A.,
Ropers H.H., von Spiczak S., Tonnies H., Villeneuve N., Villard L.,
Zabel B., Zenker M., Laube B., Reis A., Wieczorek D.,
Van Maldergem L., Kutsche K.;
"Mutations in GRIN2A and GRIN2B encoding regulatory subunits of NMDA
receptors cause variable neurodevelopmental phenotypes.";
Nat. Genet. 42:1021-1026(2010).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=26919761; DOI=10.1021/acs.jmedchem.5b02010;
Volgraf M., Sellers B.D., Jiang Y., Wu G., Ly C.Q., Villemure E.,
Pastor R.M., Yuen P.W., Lu A., Luo X., Liu M., Zhang S., Sun L.,
Fu Y., Lupardus P.J., Wallweber H.J., Liederer B.M., Deshmukh G.,
Plise E., Tay S., Reynen P., Herrington J., Gustafson A., Liu Y.,
Dirksen A., Dietz M.G., Liu Y., Wang T.M., Hanson J.E., Hackos D.,
Scearce-Levie K., Schwarz J.B.;
"Discovery of GluN2A-Selective NMDA Receptor Positive Allosteric
Modulators (PAMs): Tuning Deactivation Kinetics via Structure-Based
Design.";
J. Med. Chem. 59:2760-2779(2016).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=26875626; DOI=10.1016/j.neuron.2016.01.016;
Hackos D.H., Lupardus P.J., Grand T., Chen Y., Wang T.M., Reynen P.,
Gustafson A., Wallweber H.J., Volgraf M., Sellers B.D., Schwarz J.B.,
Paoletti P., Sheng M., Zhou Q., Hanson J.E.;
"Positive Allosteric Modulators of GluN2A-Containing NMDARs with
Distinct Modes of Action and Impacts on Circuit Function.";
Neuron 89:983-999(2016).
[12]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF MET-818.
PubMed=28126851; DOI=10.1124/mol.116.106781;
Chen W., Tankovic A., Burger P.B., Kusumoto H., Traynelis S.F.,
Yuan H.;
"Functional evaluation of a de novo GRIN2A mutation identified in a
patient with profound global developmental delay and refractory
epilepsy.";
Mol. Pharmacol. 91:317-330(2017).
[13] {ECO:0000244|PDB:5EWJ, ECO:0000244|PDB:5EWL, ECO:0000244|PDB:5EWM}
X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 31-394 IN COMPLEX WITH GRIN1
AND SYNTHETIC INHIBITOR IFENPRODIL, SUBUNIT, GLYCOSYLATION AT ASN-74
AND ASN-341, AND DISULFIDE BONDS.
PubMed=26912815; DOI=10.1124/mol.115.103036;
Stroebel D., Buhl D.L., Knafels J.D., Chanda P.K., Green M.,
Sciabola S., Mony L., Paoletti P., Pandit J.;
"A Novel Binding Mode Reveals Two Distinct Classes of NMDA Receptor
GluN2B-selective Antagonists.";
Mol. Pharmacol. 89:541-551(2016).
[14]
VARIANTS ILE-18; ASN-50; VAL-271; MET-362; VAL-825; ARG-1014;
SER-1026; ARG-1342; LEU-1415; PHE-1424 AND PHE-1452.
PubMed=22833210; DOI=10.1038/tp.2011.52;
S2D team;
Tarabeux J., Kebir O., Gauthier J., Hamdan F.F., Xiong L., Piton A.,
Spiegelman D., Henrion E., Millet B., Fathalli F., Joober R.,
Rapoport J.L., DeLisi L.E., Fombonne E., Mottron L., Forget-Dubois N.,
Boivin M., Michaud J.L., Drapeau P., Lafreniere R.G., Rouleau G.A.,
Krebs M.O.;
"Rare mutations in N-methyl-D-aspartate glutamate receptors in autism
spectrum disorders and schizophrenia.";
Transl. Psychiatry 1:E55-E55(2011).
[15]
VARIANT MRD6 LEU-553.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
[16]
VARIANT MRD6 TYR-456.
PubMed=23160955; DOI=10.1126/science.1227764;
O'Roak B.J., Vives L., Fu W., Egertson J.D., Stanaway I.B.,
Phelps I.G., Carvill G., Kumar A., Lee C., Ankenman K., Munson J.,
Hiatt J.B., Turner E.H., Levy R., O'Day D.R., Krumm N., Coe B.P.,
Martin B.K., Borenstein E., Nickerson D.A., Mefford H.C., Doherty D.,
Akey J.M., Bernier R., Eichler E.E., Shendure J.;
"Multiplex targeted sequencing identifies recurrently mutated genes in
autism spectrum disorders.";
Science 338:1619-1622(2012).
[17]
INVOLVEMENT IN EIEE27, VARIANTS EIEE27 HIS-540; ILE-615 AND GLY-618,
AND CHARACTERIZATION OF VARIANTS EIEE27 HIS-540; ILE-615 AND GLY-618.
PubMed=24272827; DOI=10.1002/ana.24073;
Lemke J.R., Hendrickx R., Geider K., Laube B., Schwake M.,
Harvey R.J., James V.M., Pepler A., Steiner I., Hortnagel K.,
Neidhardt J., Ruf S., Wolff M., Bartholdi D., Caraballo R.,
Platzer K., Suls A., De Jonghe P., Biskup S., Weckhuysen S.;
"GRIN2B mutations in West syndrome and intellectual disability with
focal epilepsy.";
Ann. Neurol. 75:147-154(2014).
[18]
VARIANT MRD6 GLY-413, AND CHARACTERIZATION OF VARIANT MRD6 GLY-413.
PubMed=24863970; DOI=10.1016/j.ymgme.2014.04.001;
Adams D.R., Yuan H., Holyoak T., Arajs K.H., Hakimi P., Markello T.C.,
Wolfe L.A., Vilboux T., Burton B.K., Fajardo K.F., Grahame G.,
Holloman C., Sincan M., Smith A.C., Wells G.A., Huang Y., Vega H.,
Snyder J.P., Golas G.A., Tifft C.J., Boerkoel C.F., Hanson R.W.,
Traynelis S.F., Kerr D.S., Gahl W.A.;
"Three rare diseases in one sib pair: RAI1, PCK1, GRIN2B mutations
associated with Smith-Magenis Syndrome, cytosolic PEPCK deficiency and
NMDA receptor glutamate insensitivity.";
Mol. Genet. Metab. 113:161-170(2014).
[19]
VARIANT MRD6 GLU-820.
PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C.,
Patry L., Massicotte C., Ambalavanan A., Spiegelman D., Diallo O.,
Henrion E., Dionne-Laporte A., Fougerat A., Pshezhetsky A.V.,
Venkateswaran S., Rouleau G.A., Michaud J.L.;
"De novo mutations in moderate or severe intellectual disability.";
PLoS Genet. 10:E1004772-E1004772(2014).
[20]
VARIANTS MRD6 ARG-436; PHE-461 AND HIS-696, CHARACTERIZATION OF
VARIANTS MRD6 GLY-413; ARG-436; TYR-456; PHE-461; CYS-682 AND HIS-696,
AND CHARACTERIZATION OF VARIANT EIEE27 HIS-540.
PubMed=27839871; DOI=10.1016/j.ajhg.2016.10.002;
Swanger S.A., Chen W., Wells G., Burger P.B., Tankovic A.,
Bhattacharya S., Strong K.L., Hu C., Kusumoto H., Zhang J.,
Adams D.R., Millichap J.J., Petrovski S., Traynelis S.F., Yuan H.;
"Mechanistic insight into NMDA receptor dysregulation by rare variants
in the GluN2A and GluN2B agonist binding domains.";
Am. J. Hum. Genet. 99:1261-1280(2016).
[21]
VARIANT EIEE27 MET-15, AND VARIANT ALA-1439.
PubMed=27864847; DOI=10.1002/humu.23149;
Clinical Study Group;
Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D.,
Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D.,
Bigoni S., Barba C., Mari F., Montomoli M., Pisano T., Rosati A.,
Guerrini R.;
"Diagnostic targeted resequencing in 349 patients with drug-resistant
pediatric epilepsies identifies causative mutations in 30 different
genes.";
Hum. Mutat. 38:216-225(2017).
[22]
CHARACTERIZATION OF VARIANT MRD6 LEU-553, AND MUTAGENESIS OF PRO-553.
PubMed=28095420; DOI=10.1371/journal.pgen.1006536;
Ogden K.K., Chen W., Swanger S.A., McDaniel M.J., Fan L.Z., Hu C.,
Tankovic A., Kusumoto H., Kosobucki G.J., Schulien A.J., Su Z.,
Pecha J., Bhattacharya S., Petrovski S., Cohen A.E., Aizenman E.,
Traynelis S.F., Yuan H.;
"Molecular mechanism of disease-associated mutations in the pre-M1
helix of NMDA receptors and potential rescue pharmacology.";
PLoS Genet. 13:E1006536-E1006536(2017).
-!- 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+) (PubMed:8768735, PubMed:26919761,
PubMed:26875626, PubMed:28126851). Sensitivity to glutamate and
channel kinetics depend on the subunit composition
(PubMed:8768735, PubMed:26875626). In concert with DAPK1 at
extrasynaptic sites, acts as a central mediator for stroke damage.
Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA
receptor channel activity inducing injurious Ca2+ influx through
them, resulting in an irreversible neuronal death. Contributes to
neural pattern formation in the developing brain. Plays a role in
long-term depression (LTD) of hippocampus membrane currents and in
synaptic plasticity (By similarity).
{ECO:0000250|UniProtKB:Q01097, ECO:0000269|PubMed:26875626,
ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:28126851,
ECO:0000269|PubMed:8768735}.
-!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed
of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A,
GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:8768735,
PubMed:26919761, PubMed:26875626, PubMed:28126851,
PubMed:26912815). Can also form heterotetrameric channels that
contain at least one zeta subunit (GRIN1), at least one epsilon
subunit, plus GRIN3A or GRIN3B (By similarity). In vivo, the
subunit composition may depend on the expression levels of the
different subunits (Probable). Found in a complex with GRIN1 and
GRIN3B. Found in a complex with GRIN1, GRIN3A and PPP2CB.
Interacts with PDZ domains of PATJ, DLG3 and DLG4. Interacts with
HIP1 and NETO1 (By similarity). Interacts with MAGI3
(PubMed:10748157). Interacts with DAPK1 (By similarity). Found in
a complex with GRIN1 and PRR7 (PubMed:27458189). Interacts with
PRR7 (PubMed:27458189). {ECO:0000250|UniProtKB:Q00960,
ECO:0000250|UniProtKB:Q01097, ECO:0000269|PubMed:10748157,
ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:26912815,
ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:27458189,
ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:8768735}.
-!- INTERACTION:
Q9UQM7:CAMK2A; NbExp=3; IntAct=EBI-2256942, EBI-1383687;
Q62936:Dlg3 (xeno); NbExp=4; IntAct=EBI-2256942, EBI-349596;
P78352:DLG4; NbExp=3; IntAct=EBI-2256942, EBI-80389;
P31016:Dlg4 (xeno); NbExp=2; IntAct=EBI-2256942, EBI-375655;
P62139:PPP1CA (xeno); NbExp=2; IntAct=EBI-2256942, EBI-2008988;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26875626,
ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:28126851,
ECO:0000269|PubMed:8768735}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q00960}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00960}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:Q00960}.
-!- TISSUE SPECIFICITY: Primarily found in the fronto-parieto-temporal
cortex and hippocampus pyramidal cells, lower expression in the
basal ganglia. {ECO:0000269|PubMed:9547169}.
-!- 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:Q00960}.
-!- PTM: Phosphorylated on tyrosine residues (By similarity).
Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA
receptor channel activity (By similarity).
{ECO:0000250|UniProtKB:Q00960, ECO:0000250|UniProtKB:Q01097}.
-!- DISEASE: Mental retardation, autosomal dominant 6, with or without
seizures (MRD6) [MIM:613970]: A disorder characterized by
significantly below average general intellectual functioning
associated with impairments in adaptive behavior and manifested
during the developmental period. MRD6 additional features may
include seizures, hypotonia, abnormal movements, such as dystonia,
and autistic features. {ECO:0000269|PubMed:20890276,
ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:23160955,
ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:25356899,
ECO:0000269|PubMed:27839871, ECO:0000269|PubMed:28095420}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Epileptic encephalopathy, early infantile, 27 (EIEE27)
[MIM:616139]: A form of epileptic encephalopathy, a heterogeneous
group of severe childhood onset epilepsies characterized by
refractory seizures, neurodevelopmental impairment, and poor
prognosis. Development is normal prior to seizure onset, after
which cognitive and motor delays become apparent.
{ECO:0000269|PubMed:24272827, ECO:0000269|PubMed:27839871,
ECO:0000269|PubMed:27864847}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=A chromosomal aberrations involving GRIN2B has been
found in patients with mental retardation. Translocations
t(9;12)(p23;p13.1) and t(10;12)(q21.1;p13.1) with a common
breakpoint in 12p13.1.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR2B/GRIN2B subfamily. {ECO:0000305}.
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EMBL; U90278; AAB49993.1; -; mRNA.
EMBL; U88963; AAD00659.1; -; mRNA.
EMBL; U11287; AAB60368.1; -; mRNA.
EMBL; BC113618; AAI13619.1; -; mRNA.
EMBL; BC113620; AAI13621.1; -; mRNA.
EMBL; U28758; AAA74930.1; -; mRNA.
EMBL; U28861; AAA69919.1; -; mRNA.
EMBL; U28862; AAA69920.1; -; mRNA.
CCDS; CCDS8662.1; -.
PIR; I39066; I39066.
PIR; S52086; S52086.
RefSeq; NP_000825.2; NM_000834.3.
RefSeq; XP_011518930.1; XM_011520628.2.
RefSeq; XP_011518931.1; XM_011520629.2.
RefSeq; XP_016874708.1; XM_017019219.1.
UniGene; Hs.504844; -.
UniGene; Hs.632856; -.
UniGene; Hs.654430; -.
PDB; 1S11; Model; -; A=403-543, B=660-801.
PDB; 1S2S; Model; -; A=405-543, B=660-801.
PDB; 2IPV; Model; -; X=404-768.
PDB; 5EWJ; X-ray; 2.77 A; B/D=31-394.
PDB; 5EWL; X-ray; 2.98 A; B/D=31-394.
PDB; 5EWM; X-ray; 2.76 A; B/D=31-394.
PDBsum; 1S11; -.
PDBsum; 1S2S; -.
PDBsum; 2IPV; -.
PDBsum; 5EWJ; -.
PDBsum; 5EWL; -.
PDBsum; 5EWM; -.
ProteinModelPortal; Q13224; -.
SMR; Q13224; -.
BioGrid; 109161; 26.
DIP; DIP-41002N; -.
IntAct; Q13224; 14.
MINT; Q13224; -.
STRING; 9606.ENSP00000279593; -.
BindingDB; Q13224; -.
ChEMBL; CHEMBL1904; -.
DrugBank; DB00659; Acamprosate.
DrugBank; DB06151; Acetylcysteine.
DrugBank; DB00289; Atomoxetine.
DrugBank; DB00949; Felbamate.
DrugBank; DB00996; Gabapentin.
DrugBank; DB06741; Gavestinel.
DrugBank; DB00502; Haloperidol.
DrugBank; DB08954; Ifenprodil.
DrugBank; DB06738; Ketobemidone.
DrugBank; DB00142; L-Glutamic Acid.
DrugBank; DB01043; Memantine.
DrugBank; DB04896; Milnacipran.
DrugBank; DB00312; Pentobarbital.
DrugBank; DB00454; Pethidine.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB01708; Prasterone.
DrugBank; DB00418; Secobarbital.
DrugBank; DB01520; Tenocyclidine.
iPTMnet; Q13224; -.
PhosphoSitePlus; Q13224; -.
BioMuta; GRIN2B; -.
DMDM; 14548162; -.
PaxDb; Q13224; -.
PeptideAtlas; Q13224; -.
PRIDE; Q13224; -.
Ensembl; ENST00000609686; ENSP00000477455; ENSG00000273079.
GeneID; 2904; -.
KEGG; hsa:2904; -.
UCSC; uc001rbt.3; human.
CTD; 2904; -.
DisGeNET; 2904; -.
EuPathDB; HostDB:ENSG00000273079.4; -.
GeneCards; GRIN2B; -.
H-InvDB; HIX0036873; -.
HGNC; HGNC:4586; GRIN2B.
HPA; HPA069762; -.
MalaCards; GRIN2B; -.
MIM; 138252; gene.
MIM; 613970; phenotype.
MIM; 616139; phenotype.
neXtProt; NX_Q13224; -.
OpenTargets; ENSG00000273079; -.
Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
Orphanet; 3451; West syndrome.
PharmGKB; PA28980; -.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
GeneTree; ENSGT00910000143978; -.
HOGENOM; HOG000113802; -.
HOVERGEN; HBG052635; -.
InParanoid; Q13224; -.
KO; K05210; -.
OMA; RNNYPEM; -.
OrthoDB; EOG091G09KH; -.
PhylomeDB; Q13224; -.
TreeFam; TF314731; -.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-HSA-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6794361; Neurexins and neuroligins.
Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
Reactome; R-HSA-9032500; Activated NTRK2 signals through FYN.
SignaLink; Q13224; -.
SIGNOR; Q13224; -.
ChiTaRS; GRIN2B; human.
GeneWiki; GRIN2B; -.
GenomeRNAi; 2904; -.
PRO; PR:Q13224; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000273079; -.
CleanEx; HS_GRIN2B; -.
ExpressionAtlas; Q13224; baseline and differential.
Genevisible; Q13224; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; ISS:ARUK-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; ISS:ARUK-UCL.
GO; GO:0043005; C:neuron projection; ISS:BHF-UCL.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; TAS:ARUK-UCL.
GO; GO:0097060; C:synaptic membrane; ISS:ARUK-UCL.
GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0016595; F:glutamate binding; ISS:UniProtKB.
GO; GO:0022849; F:glutamate-gated calcium ion channel activity; IDA:UniProtKB.
GO; GO:0016594; F:glycine binding; IDA:UniProtKB.
GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0007420; P:brain development; NAS:ARUK-UCL.
GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IDA:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0098976; P:excitatory chemical synaptic transmission; NAS:ARUK-UCL.
GO; GO:0007215; P:glutamate receptor signaling pathway; TAS:ProtInc.
GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0007275; P:multicellular organism development; TAS:ARUK-UCL.
GO; GO:1902951; P:negative regulation of dendritic spine maintenance; ISS:ARUK-UCL.
GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; ISS:ARUK-UCL.
GO; GO:1901216; P:positive regulation of neuron death; ISS:ARUK-UCL.
GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; NAS:ARUK-UCL.
GO; GO:0045471; P:response to ethanol; IDA:UniProtKB.
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;
Chromosomal rearrangement; Complete proteome; Disease mutation;
Disulfide bond; Epilepsy; Glycoprotein; Ion channel; Ion transport;
Ligand-gated ion channel; Magnesium; Membrane; Mental retardation;
Metal-binding; Phosphoprotein; Polymorphism;
Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
Synapse; Transmembrane; Transmembrane helix; Transport; Zinc.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 1484 Glutamate receptor ionotropic, NMDA 2B.
/FTId=PRO_0000011577.
TOPO_DOM 27 557 Extracellular.
{ECO:0000250|UniProtKB:Q00960}.
TRANSMEM 558 576 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 577 603 Cytoplasmic.
{ECO:0000250|UniProtKB:Q00960}.
INTRAMEM 604 623 Discontinuously helical.
{ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 624 630 Cytoplasmic.
{ECO:0000250|UniProtKB:Q00960}.
TRANSMEM 631 646 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 647 817 Extracellular.
{ECO:0000250|UniProtKB:Q00960}.
TRANSMEM 818 837 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 838 1484 Cytoplasmic.
{ECO:0000250|UniProtKB:Q00960}.
REGION 604 623 Pore-forming.
{ECO:0000250|UniProtKB:A7XY94}.
REGION 690 691 Glutamate binding.
{ECO:0000250|UniProtKB:Q00960}.
REGION 1292 1304 Interaction with DAPK1.
{ECO:0000250|UniProtKB:Q01097}.
MOTIF 1482 1484 PDZ-binding. {ECO:0000250}.
COMPBIAS 984 989 Poly-His.
COMPBIAS 1361 1364 Poly-His.
METAL 127 127 Zinc. {ECO:0000250|UniProtKB:Q00960}.
METAL 284 284 Zinc. {ECO:0000250|UniProtKB:Q00960}.
BINDING 514 514 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
BINDING 519 519 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
BINDING 732 732 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
SITE 615 615 Functional determinant of NMDA receptors.
{ECO:0000250}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 886 886 Phosphoserine.
{ECO:0000250|UniProtKB:Q00960}.
MOD_RES 917 917 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 920 920 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 962 962 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1039 1039 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1058 1058 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1061 1061 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1064 1064 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1109 1109 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1133 1133 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1143 1143 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1155 1155 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1255 1255 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1259 1259 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1303 1303 Phosphoserine; by DAPK1.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1474 1474 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01097}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 348 348 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 542 542 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 688 688 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 86 321 {ECO:0000250|UniProtKB:Q00960}.
DISULFID 429 456 {ECO:0000250|UniProtKB:Q00960}.
DISULFID 436 457 {ECO:0000250|UniProtKB:Q00960}.
DISULFID 746 801 {ECO:0000250|UniProtKB:Q00960}.
VARIANT 15 15 V -> M (in EIEE27; unknown pathological
significance; dbSNP:rs1057519553).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078235.
VARIANT 18 18 V -> I (in dbSNP:rs201094029).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079943.
VARIANT 50 50 I -> N (found in a patient with
schizophrenia; unknown pathological
significance).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079944.
VARIANT 271 271 A -> V (in dbSNP:rs138098032).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079945.
VARIANT 362 362 L -> M (found in a patient with
schizophrenia; unknown pathological
significance).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079946.
VARIANT 407 407 S -> N. {ECO:0000269|PubMed:7999784}.
/FTId=VAR_011317.
VARIANT 413 413 E -> G (in MRD6; decreased protein
abundance; decreased localization to the
cell membrane; changed glutamate-gated
calcium ion channel activity
characterized by decreased glutamate
potency; dbSNP:rs527236034).
{ECO:0000269|PubMed:24863970,
ECO:0000269|PubMed:27839871}.
/FTId=VAR_079947.
VARIANT 436 436 C -> R (in MRD6; decreased protein
abundance; decreased localization to the
cell membrane).
{ECO:0000269|PubMed:27839871}.
/FTId=VAR_079948.
VARIANT 456 456 C -> Y (in MRD6; decreased protein
abundance; decreased localization to the
cell membrane; changed glutamate-gated
calcium ion channel activity
characterized by increased glutamate and
glycine potency and increased open
probability; dbSNP:rs397514555).
{ECO:0000269|PubMed:23160955,
ECO:0000269|PubMed:27839871}.
/FTId=VAR_076764.
VARIANT 461 461 C -> F (in MRD6; decreased protein
abundance; decreased localization to the
cell membrane; decreased glutamate-gated
calcium ion channel activity
characterized by decreased glutamate
potency and increased glycine potency).
{ECO:0000269|PubMed:27839871}.
/FTId=VAR_079949.
VARIANT 540 540 R -> H (in EIEE27; decreased protein
abundance; decreased localization to the
cell membrane; increased glutamate-gated
calcium ion channel activity via an
allosteric effect which is characterized
by increased glutamate and glycine
potency and increased open probability;
the mutant channel is less sensitive to
magnesium inhibition and has increased
calcium permeability compared to wild-
type; dbSNP:rs672601378).
{ECO:0000269|PubMed:24272827,
ECO:0000269|PubMed:27839871}.
/FTId=VAR_072663.
VARIANT 553 553 P -> L (in MRD6; no effect on
localization to the cell membrane; loss
of glutamate-gated calcium ion channel
activity; dbSNP:rs397514556).
{ECO:0000269|PubMed:23033978,
ECO:0000269|PubMed:28095420}.
/FTId=VAR_069384.
VARIANT 615 615 N -> I (in EIEE27; severe phenotype with
early onset seizures; gain of function
mutation; results in neuronal
hyperexcitability; the mutant channel is
not inhibited by magnesium and has
increased calcium permeability compared
to wild-type; dbSNP:rs672601377).
{ECO:0000269|PubMed:24272827}.
/FTId=VAR_072664.
VARIANT 618 618 V -> G (in EIEE27; severe phenotype with
early onset seizures; gain of function
mutation; results in neuronal
hyperexcitability; the mutant channel is
not inhibited by magnesium and has
increased calcium permeability compared
to wild-type; dbSNP:rs672601376).
{ECO:0000269|PubMed:24272827}.
/FTId=VAR_072665.
VARIANT 682 682 R -> C (in MRD6; decreased protein
abundance; no effect on localization to
the cell membrane; no significant effect
on calcium ion transmembrane import into
cytosol; analysis of agonist dose-
response curves for glutamate and glycine
are not consistent; dbSNP:rs387906636).
{ECO:0000269|PubMed:20890276,
ECO:0000269|PubMed:27839871}.
/FTId=VAR_065900.
VARIANT 696 696 R -> H (in MRD6; decreased protein
abundance; decreased localization to the
cell membrane; changed glutamate-gated
calcium ion channel activity
characterized by increased glutamate and
glycine potency).
{ECO:0000269|PubMed:27839871}.
/FTId=VAR_079950.
VARIANT 820 820 G -> E (in MRD6).
{ECO:0000269|PubMed:25356899}.
/FTId=VAR_078647.
VARIANT 825 825 L -> V (probable disease-associated
mutation found in a patient with autism
spectrum disorder).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079951.
VARIANT 1014 1014 Q -> R (found in a patient with
schizophrenia; unknown pathological
significance).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079952.
VARIANT 1026 1026 G -> S (in dbSNP:rs201963596).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079953.
VARIANT 1342 1342 M -> R. {ECO:0000269|PubMed:22833210}.
/FTId=VAR_079954.
VARIANT 1415 1415 S -> L (found in a patient with autism
spectrum disorder; unknown pathological
significance; dbSNP:rs201463390).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079955.
VARIANT 1424 1424 L -> F (in dbSNP:rs748128078).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079956.
VARIANT 1439 1439 P -> A (found in a patient with Landau-
Kleffner syndrome; unknown pathological
significance; dbSNP:rs758042475).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078236.
VARIANT 1452 1452 S -> F (found in a patient with
schizophrenia; unknown pathological
significance; dbSNP:rs756790727).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079957.
MUTAGEN 553 553 P->R: Changed glutamate-gated calcium ion
channel activity characterized by
increased glutamate and glycine potency
and slowed response rise time and
deactivation time course.
{ECO:0000269|PubMed:28095420}.
MUTAGEN 818 818 M->V: Increased glutamate and glycine
agonist potency.
{ECO:0000269|PubMed:28126851}.
CONFLICT 434 434 V -> A (in Ref. 3; AAD00659).
{ECO:0000305}.
CONFLICT 745 745 G -> A (in Ref. 5; AAA69920).
{ECO:0000305}.
CONFLICT 773 773 K -> N (in Ref. 5; AAA69920/AAA74930).
{ECO:0000305}.
CONFLICT 796 796 W -> C (in Ref. 5; AAA69920/AAA74930).
{ECO:0000305}.
CONFLICT 888 888 T -> P (in Ref. 5; AAA69920/AAA74930).
{ECO:0000305}.
CONFLICT 902 902 L -> V (in Ref. 5; AAA69920/AAA74930).
{ECO:0000305}.
CONFLICT 920 921 SA -> RP (in Ref. 1; AAB60368).
{ECO:0000305}.
CONFLICT 958 958 L -> S (in Ref. 5; AAA69920/AAA74930).
{ECO:0000305}.
CONFLICT 980 982 VYQ -> DHY (in Ref. 5; AAA69920).
{ECO:0000305}.
CONFLICT 1056 1056 I -> M (in Ref. 5; AAA69920).
{ECO:0000305}.
CONFLICT 1167 1167 V -> I (in Ref. 2; AAB49993).
{ECO:0000305}.
STRAND 34 44 {ECO:0000244|PDB:5EWM}.
HELIX 47 50 {ECO:0000244|PDB:5EWM}.
STRAND 62 73 {ECO:0000244|PDB:5EWM}.
HELIX 78 91 {ECO:0000244|PDB:5EWM}.
STRAND 94 100 {ECO:0000244|PDB:5EWM}.
HELIX 107 119 {ECO:0000244|PDB:5EWM}.
STRAND 123 127 {ECO:0000244|PDB:5EWM}.
HELIX 128 131 {ECO:0000244|PDB:5EWM}.
STRAND 143 147 {ECO:0000244|PDB:5EWM}.
HELIX 150 164 {ECO:0000244|PDB:5EWM}.
STRAND 168 173 {ECO:0000244|PDB:5EWM}.
HELIX 179 191 {ECO:0000244|PDB:5EWM}.
STRAND 193 195 {ECO:0000244|PDB:5EWL}.
STRAND 198 204 {ECO:0000244|PDB:5EWM}.
HELIX 215 221 {ECO:0000244|PDB:5EWM}.
STRAND 226 232 {ECO:0000244|PDB:5EWM}.
HELIX 234 246 {ECO:0000244|PDB:5EWM}.
STRAND 255 258 {ECO:0000244|PDB:5EWM}.
HELIX 260 263 {ECO:0000244|PDB:5EWM}.
STRAND 278 282 {ECO:0000244|PDB:5EWM}.
TURN 284 286 {ECO:0000244|PDB:5EWM}.
HELIX 289 311 {ECO:0000244|PDB:5EWM}.
STRAND 321 323 {ECO:0000244|PDB:5EWJ}.
HELIX 324 327 {ECO:0000244|PDB:5EWM}.
HELIX 328 330 {ECO:0000244|PDB:5EWM}.
HELIX 336 339 {ECO:0000244|PDB:5EWM}.
STRAND 355 359 {ECO:0000244|PDB:5EWM}.
STRAND 362 367 {ECO:0000244|PDB:5EWM}.
STRAND 373 379 {ECO:0000244|PDB:5EWM}.
STRAND 384 387 {ECO:0000244|PDB:5EWM}.
SEQUENCE 1484 AA; 166367 MW; 40AEB12BE6E50CEF CRC64;
MKPRAECCSP KFWLVLAVLA VSGSRARSQK SPPSIGIAVI LVGTSDEVAI KDAHEKDDFH
HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVFA DDTDQEAIAQ ILDFISAQTL
TPILGIHGGS SMIMADKDES SMFFQFGPSI EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ
DFVNKIRSTI ENSFVGWELE EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI
FEVANSVGLT GYGYTWIVPS LVAGDTDTVP AEFPTGLISV SYDEWDYGLP ARVRDGIAII
TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS FSEDGYQMHP
KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE QEDDHLSIVT LEEAPFVIVE
SVDPLSGTCM RNTVPCQKRI VTENKTDEEP GYIKKCCKGF CIDILKKISK SVKFTYDLYL
VTNGKHGKKI NGTWNGMIGE VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR
SNGTVSPSAF LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF
TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL AAFMIQEEYV
DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA EMHAYMGKFN QRGVDDALLS
LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT IGSGKVFAST GYGIAIQKDS GWKRQVDLAI
LQLFGDGEME ELEALWLTGI CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH
LFYWQFRHCF MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR
LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN NPPCEENLFS
DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSASSI DGLYDCDNPP FTTQSRSISK
KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS GHDDLIRSDV SDISTHTVTY GNIEGNAAKR
RKQQYKDSLK KRPASAKSRR EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK
ENSPHWEHVD LTDIYKERSD DFKRDSVSGG GPCTNRSHIK HGTGDKHGVV SGVPAPWEKN
LTNVEWEDRS GGNFCRSCPS KLHNYSTTVT GQNSGRQACI RCEACKKAGN LYDISEDNSL
QELDQPAAPV AVTSNASTTK YPQSPTNSKA QKKNRNKLRR QHSYDTFVDL QKEEAALAPR
SVSLKDKGRF MDGSPYAHMF EMSAGESTFA NNKSSVPTAG HHHHNNPGGG YMLSKSLYPD
RVTQNPFIPT FGDDQCLLHG SKSYFFRQPT VAGASKARPD FRALVTNKPV VSALHGAVPA
RFQKDICIGN QSNPCVPNNK NPRAFNGSSN GHVYEKLSSI ESDV


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18-373-88008 Glutamate [NMDA] receptor subunit zeta 1 - N-methyl-D-aspartate receptor subunit NR1 Polyclonal 0.5 ml
18-373-88024 Glutamate [NMDA] receptor subunit zeta 1 - N-methyl-D-aspartate receptor subunit NR1 Polyclonal 0.5 ml


 

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