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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) (hNR2A)

 NMDE1_HUMAN             Reviewed;        1464 AA.
Q12879; O00669; Q17RZ6;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 185.
RecName: Full=Glutamate receptor ionotropic, NMDA 2A;
Short=GluN2A;
AltName: Full=Glutamate [NMDA] receptor subunit epsilon-1;
AltName: Full=N-methyl D-aspartate receptor subtype 2A;
Short=NMDAR2A {ECO:0000303|PubMed:8768735};
Short=NR2A;
Short=hNR2A {ECO:0000303|PubMed:8061049};
Flags: Precursor;
Name=GRIN2A; Synonyms=NMDAR2A;
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), AND VARIANT GLU-270.
PubMed=8061049; DOI=10.1016/0167-4889(94)90086-8;
Foldes R.L., Adams S.L., Fantaske R.P., Kamboj R.K.;
"Human N-methyl-D-aspartate receptor modulatory subunit hNR2A: cloning
and sequencing of the cDNA and primary structure of the protein.";
Biochim. Biophys. Acta 1223:155-159(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND SUBUNIT.
TISSUE=Cerebellum;
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 [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[5] {ECO:0000244|PDB:5I2K, ECO:0000244|PDB:5I2N, ECO:0000244|PDB:5KDT}
X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 401-539 AND 566-800 IN
COMPLEX WITH GLUTAMATE AND GRIN1, FUNCTION, SUBCELLULAR LOCATION,
SUBUNIT, AND DISULFIDE BONDS.
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).
[6] {ECO:0000244|PDB:5H8F, ECO:0000244|PDB:5H8H, ECO:0000244|PDB:5H8N, ECO:0000244|PDB:5H8Q, ECO:0000244|PDB:5KCJ}
X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 401-539 AND 566-800 IN
COMPLEX WITH GLUTAMATE AND GRIN1, FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, AND DISULFIDE BONDS.
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).
[7] {ECO:0000244|PDB:5TP9, ECO:0000244|PDB:5TPA}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 401-539 AND 566-800 IN
COMPLEX WITH GRIN1 AND GLUTAMATE, SUBCELLULAR LOCATION, SUBUNIT,
FUNCTION, AND DISULFIDE BONDS.
PubMed=28105280; DOI=10.1021/acsmedchemlett.6b00388;
Villemure E., Volgraf M., Jiang Y., Wu G., Ly C.Q., Yuen P.W., Lu A.,
Luo X., Liu M., Zhang S., Lupardus P.J., Wallweber H.J.,
Liederer B.M., Deshmukh G., Plise E., Tay S., Wang T.M., Hanson J.E.,
Hackos D.H., Scearce-Levie K., Schwarz J.B., Sellers B.D.;
"GluN2A-Selective Pyridopyrimidinone Series of NMDAR Positive
Allosteric Modulators with an Improved in Vivo Profile.";
ACS Med. Chem. Lett. 8:84-89(2017).
[8]
CHROMOSOMAL TRANSLOCATION, VARIANT FESD LYS-615, AND CHARACTERIZATION
OF VARIANT FESD LYS-615.
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).
[9]
PROBABLE INVOLVEMENT IN MELANOMA, AND VARIANTS LEU-57; ILE-183;
ASN-252; PHE-278; LYS-371; LYS-373; GLU-449; SER-459; ARG-595;
PHE-598; ILE-653; GLU-712; TRP-740; GLU-889; LYS-920; PHE-929;
LYS-962; LYS-1073; LEU-1074; ASN-1153; LYS-1175; GLY-1276; LYS-1285;
TRP-1318; LEU-1366; ASN-1421; LEU-1425; LYS-1426 AND CYS-1462.
PubMed=21499247; DOI=10.1038/ng.810;
Wei X., Walia V., Lin J.C., Teer J.K., Prickett T.D., Gartner J.,
Davis S., Stemke-Hale K., Davies M.A., Gershenwald J.E., Robinson W.,
Robinson S., Rosenberg S.A., Samuels Y.;
"Exome sequencing identifies GRIN2A as frequently mutated in
melanoma.";
Nat. Genet. 43:442-446(2011).
[10]
VARIANTS FESD ARG-552 AND VAL-649.
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).
[11]
VARIANTS FESD SER-184; SER-295; ARG-483; TRP-504; HIS-518; THR-548;
VAL-652; ASN-669; THR-694; THR-716; ASN-731; ASN-933 AND ASN-1251,
VARIANT GLY-1276, AND CHARACTERIZATION OF VARIANTS FESD HIS-518 AND
VAL-652.
PubMed=23933820; DOI=10.1038/ng.2726;
Lesca G., Rudolf G., Bruneau N., Lozovaya N., Labalme A.,
Boutry-Kryza N., Salmi M., Tsintsadze T., Addis L., Motte J.,
Wright S., Tsintsadze V., Michel A., Doummar D., Lascelles K.,
Strug L., Waters P., de Bellescize J., Vrielynck P.,
de Saint Martin A., Ville D., Ryvlin P., Arzimanoglou A., Hirsch E.,
Vincent A., Pal D., Burnashev N., Sanlaville D., Szepetowski P.;
"GRIN2A mutations in acquired epileptic aphasia and related childhood
focal epilepsies and encephalopathies with speech and language
dysfunction.";
Nat. Genet. 45:1061-1066(2013).
[12]
VARIANTS FESD ARG-79; TYR-231; VAL-243; VAL-290; TRP-370; ARG-436;
SER-547 DEL; SER-699; VAL-705; LYS-714; THR-727; LEU-734; GLU-772;
THR-814; PHE-904 AND SER-976, VARIANT ILE-183, AND CHARACTERIZATION OF
VARIANT FESD VAL-243.
PubMed=23933819; DOI=10.1038/ng.2728;
Lemke J.R., Lal D., Reinthaler E.M., Steiner I., Nothnagel M.,
Alber M., Geider K., Laube B., Schwake M., Finsterwalder K.,
Franke A., Schilhabel M., Jahn J.A., Muhle H., Boor R.,
Van Paesschen W., Caraballo R., Fejerman N., Weckhuysen S.,
De Jonghe P., Larsen J., Moller R.S., Hjalgrim H., Addis L., Tang S.,
Hughes E., Pal D.K., Veri K., Vaher U., Talvik T., Dimova P.,
Guerrero Lopez R., Serratosa J.M., Linnankivi T., Lehesjoki A.E.,
Ruf S., Wolff M., Buerki S., Wohlrab G., Kroell J., Datta A.N.,
Fiedler B., Kurlemann G., Kluger G., Hahn A., Haberlandt D.E.,
Kutzer C., Sperner J., Becker F., Weber Y.G., Feucht M., Steinbock H.,
Neophythou B., Ronen G.M., Gruber-Sedlmayr U., Geldner J.,
Harvey R.J., Hoffmann P., Herms S., Altmuller J., Toliat M.R.,
Thiele H., Nurnberg P., Wilhelm C., Stephani U., Helbig I., Lerche H.,
Zimprich F., Neubauer B.A., Biskup S., von Spiczak S.;
"Mutations in GRIN2A cause idiopathic focal epilepsy with rolandic
spikes.";
Nat. Genet. 45:1067-1072(2013).
[13]
VARIANT FESD MET-531, AND CHARACTERIZATION OF VARIANT FESD MET-531.
PubMed=23933818; DOI=10.1038/ng.2727;
Carvill G.L., Regan B.M., Yendle S.C., O'Roak B.J., Lozovaya N.,
Bruneau N., Burnashev N., Khan A., Cook J., Geraghty E., Sadleir L.G.,
Turner S.J., Tsai M.H., Webster R., Ouvrier R., Damiano J.A.,
Berkovic S.F., Shendure J., Hildebrand M.S., Szepetowski P.,
Scheffer I.E., Mefford H.C.;
"GRIN2A mutations cause epilepsy-aphasia spectrum disorders.";
Nat. Genet. 45:1073-1076(2013).
[14]
PROBABLE INVOLVEMENT IN MELANOMA, AND VARIANTS PHE-349; ALA-762;
GLU-889; LEU-1132 AND SER-1133.
PubMed=24455489; DOI=10.3389/fonc.2013.00333;
D'mello S.A., Flanagan J.U., Green T.N., Leung E.Y.,
Askarian-Amiri M.E., Joseph W.R., McCrystal M.R., Isaacs R.J.,
Shaw J.H., Furneaux C.E., During M.J., Finlay G.J., Baguley B.C.,
Kalev-Zylinska M.L.;
"Evidence that GRIN2A mutations in melanoma correlate with decreased
survival.";
Front. Oncol. 3:333-333(2014).
[15]
VARIANT FESD VAL-817.
PubMed=24903190; DOI=10.1111/epi.12663;
FORGE Canada Consortium;
Venkateswaran S., Myers K.A., Smith A.C., Beaulieu C.L.,
Schwartzentruber J.A., Majewski J., Bulman D., Boycott K.M.,
Dyment D.A.;
"Whole-exome sequencing in an individual with severe global
developmental delay and intractable epilepsy identifies a novel, de
novo GRIN2A mutation.";
Epilepsia 55:E75-E79(2014).
[16]
VARIANT FESD MET-812, AND CHARACTERIZATION OF VARIANT FESD MET-812.
PubMed=24504326; DOI=10.1038/ncomms4251;
Yuan H., Hansen K.B., Zhang J., Pierson T.M., Markello T.C.,
Fajardo K.V., Holloman C.M., Golas G., Adams D.R., Boerkoel C.F.,
Gahl W.A., Traynelis S.F.;
"Functional analysis of a de novo GRIN2A missense mutation associated
with early-onset epileptic encephalopathy.";
Nat. Commun. 5:3251-3251(2014).
[17]
VARIANT ASN-884.
PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009;
D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T.,
Sestan N., Walsh C.A.;
"Targeted DNA Sequencing from Autism Spectrum Disorder Brains
Implicates Multiple Genetic Mechanisms.";
Neuron 88:910-917(2015).
[18]
VARIANTS ASP-380; SER-989 AND GLY-1276, AND VARIANT FESD ASP-716.
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).
[19]
CHARACTERIZATION OF VARIANT FESD VAL-817.
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).
[20]
VARIANT FESD ASN-731, AND CHARACTERIZATION OF VARIANT FESD ASN-731.
PubMed=28182669; DOI=10.1371/journal.pone.0170818;
Gao K., Tankovic A., Zhang Y., Kusumoto H., Zhang J., Chen W.,
XiangWei W., Shaulsky G.H., Hu C., Traynelis S.F., Yuan H., Jiang Y.;
"A de novo loss-of-function GRIN2A mutation associated with childhood
focal epilepsy and acquired epileptic aphasia.";
PLoS ONE 12:E0170818-E0170818(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:28105280). 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:26919761, PubMed:26875626). Contributes to the slow phase
of excitatory postsynaptic current, long-term synaptic
potentiation, and learning (By similarity).
{ECO:0000250|UniProtKB:P35436, ECO:0000250|UniProtKB:Q00959,
ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:26919761,
ECO:0000269|PubMed:28105280, 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:28105280). Can also form
heterotetrameric channels that contain at least one zeta subunit
(GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B. In
vivo, the subunit composition may depend on the expression levels
of the different subunits. Found in a complex with GRIN1, GRIN3A
and PPP2CB (By similarity). Found in a complex with GRIN1 and
GRIN3B (By similarity). Interacts with AIP1 (By similarity).
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.
Interacts with LRFN2 (By similarity).
{ECO:0000250|UniProtKB:P35436, ECO:0000250|UniProtKB:Q00959,
ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:26919761,
ECO:0000269|PubMed:28105280, ECO:0000269|PubMed:8768735}.
-!- INTERACTION:
Q62936:Dlg3 (xeno); NbExp=5; IntAct=EBI-7249937, EBI-349596;
P78352:DLG4; NbExp=5; IntAct=EBI-7249937, EBI-80389;
P31016:Dlg4 (xeno); NbExp=2; IntAct=EBI-7249937, EBI-375655;
Q07954:LRP1; NbExp=2; IntAct=EBI-7249937, EBI-1046087;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26875626,
ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:28105280,
ECO:0000269|PubMed:8768735}; Multi-pass membrane protein
{ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane
{ECO:0000250|UniProtKB:Q00959}; Multi-pass membrane protein
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q12879-1; Sequence=Displayed;
Name=2;
IsoId=Q12879-2; Sequence=VSP_044300;
-!- 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:0000250|UniProtKB:Q00959}.
-!- 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}.
-!- DISEASE: Epilepsy, focal, with speech disorder and with or without
mental retardation (FESD) [MIM:245570]: A highly variable
neurologic disorder with features ranging from severe early-onset
seizures associated with delayed psychomotor development,
persistent speech difficulties, and mental retardation to a more
benign entity characterized by childhood onset of mild or
asymptomatic seizures associated with transient speech
difficulties followed by remission of seizures in adolescence and
normal psychomotor development. The disorder encompasses several
clinical entities, including Landau-Kleffner syndrome, epileptic
encephalopathy with continuous spike and wave during slow-wave
sleep, autosomal dominant rolandic epilepsy, mental retardation
and speech dyspraxia, and benign epilepsy with centrotemporal
spikes. {ECO:0000269|PubMed:20890276, ECO:0000269|PubMed:23033978,
ECO:0000269|PubMed:23933818, ECO:0000269|PubMed:23933819,
ECO:0000269|PubMed:23933820, ECO:0000269|PubMed:24504326,
ECO:0000269|PubMed:24903190, ECO:0000269|PubMed:27864847,
ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:28182669}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=A chromosomal aberration involving GRIN2A has been
found in a family with epilepsy and neurodevelopmental defects.
Translocation t(16;17)(p13.2;q11.2).
-!- DISEASE: Note=GRIN2A somatic mutations have been frequently found
in cutaneous malignant melanoma, suggesting that the glutamate
signaling pathway may play a role in the pathogenesis of melanoma.
{ECO:0000269|PubMed:21499247, ECO:0000269|PubMed:24455489}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR2A/GRIN2A subfamily. {ECO:0000305}.
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EMBL; U09002; AAB60343.1; -; mRNA.
EMBL; U90277; AAB49992.1; -; mRNA.
EMBL; AC006531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC026423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC133565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC117131; AAI17132.1; -; mRNA.
EMBL; BC143273; AAI43274.1; -; mRNA.
CCDS; CCDS10539.1; -. [Q12879-1]
CCDS; CCDS45407.1; -. [Q12879-2]
PIR; S47555; S47555.
RefSeq; NP_000824.1; NM_000833.4. [Q12879-1]
RefSeq; NP_001127879.1; NM_001134407.2. [Q12879-1]
RefSeq; NP_001127880.1; NM_001134408.2. [Q12879-2]
RefSeq; XP_011520763.1; XM_011522461.2. [Q12879-2]
UniGene; Hs.411472; -.
PDB; 3NFL; X-ray; 1.91 A; E/F/G/H=1449-1464.
PDB; 5H8F; X-ray; 1.81 A; A=401-539, A=661-802.
PDB; 5H8H; X-ray; 2.23 A; A=401-539, A=661-802.
PDB; 5H8N; X-ray; 2.50 A; A=401-539, A=661-802.
PDB; 5H8Q; X-ray; 1.90 A; A=401-539, A=661-802.
PDB; 5I2K; X-ray; 2.86 A; A=401-539, A=661-802.
PDB; 5I2N; X-ray; 2.12 A; A=401-539, A=661-802.
PDB; 5KCJ; X-ray; 2.09 A; A=401-539, A=661-802.
PDB; 5KDT; X-ray; 2.44 A; A=401-539, A=661-802.
PDB; 5TP9; X-ray; 2.40 A; A=401-539, A=661-802.
PDB; 5TPA; X-ray; 2.48 A; A=401-539, A=661-802.
PDBsum; 3NFL; -.
PDBsum; 5H8F; -.
PDBsum; 5H8H; -.
PDBsum; 5H8N; -.
PDBsum; 5H8Q; -.
PDBsum; 5I2K; -.
PDBsum; 5I2N; -.
PDBsum; 5KCJ; -.
PDBsum; 5KDT; -.
PDBsum; 5TP9; -.
PDBsum; 5TPA; -.
ProteinModelPortal; Q12879; -.
SMR; Q12879; -.
BioGrid; 109160; 49.
CORUM; Q12879; -.
DIP; DIP-40798N; -.
IntAct; Q12879; 6.
MINT; MINT-414776; -.
STRING; 9606.ENSP00000332549; -.
BindingDB; Q12879; -.
ChEMBL; CHEMBL1972; -.
DrugBank; DB00659; Acamprosate.
DrugBank; DB06151; Acetylcysteine.
DrugBank; DB00289; Atomoxetine.
DrugBank; DB00949; Felbamate.
DrugBank; DB00996; Gabapentin.
DrugBank; DB06741; Gavestinel.
DrugBank; DB00145; Glycine.
DrugBank; DB01159; Halothane.
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.
GuidetoPHARMACOLOGY; 456; -.
TCDB; 1.A.10.1.20; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
iPTMnet; Q12879; -.
PhosphoSitePlus; Q12879; -.
BioMuta; GRIN2A; -.
DMDM; 14285603; -.
EPD; Q12879; -.
PaxDb; Q12879; -.
PeptideAtlas; Q12879; -.
PRIDE; Q12879; -.
DNASU; 2903; -.
Ensembl; ENST00000330684; ENSP00000332549; ENSG00000183454. [Q12879-1]
Ensembl; ENST00000396573; ENSP00000379818; ENSG00000183454. [Q12879-1]
Ensembl; ENST00000562109; ENSP00000454998; ENSG00000183454. [Q12879-2]
GeneID; 2903; -.
KEGG; hsa:2903; -.
UCSC; uc002czr.5; human. [Q12879-1]
CTD; 2903; -.
DisGeNET; 2903; -.
EuPathDB; HostDB:ENSG00000183454.14; -.
GeneCards; GRIN2A; -.
HGNC; HGNC:4585; GRIN2A.
HPA; CAB022725; -.
MalaCards; GRIN2A; -.
MIM; 138253; gene.
MIM; 245570; phenotype.
neXtProt; NX_Q12879; -.
OpenTargets; ENSG00000183454; -.
Orphanet; 725; Continuous spikes and waves during sleep.
Orphanet; 289266; Early-onset epileptic encephalopathy and intellectual disability due to GRIN2A mutation.
Orphanet; 98818; Landau-Kleffner syndrome.
Orphanet; 1945; Rolandic epilepsy.
Orphanet; 163721; Rolandic epilepsy - speech dyspraxia.
PharmGKB; PA28979; -.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
GeneTree; ENSGT00760000119186; -.
HOGENOM; HOG000113802; -.
HOVERGEN; HBG052635; -.
InParanoid; Q12879; -.
KO; K05209; -.
OMA; HSFVRWD; -.
OrthoDB; EOG091G09KH; -.
PhylomeDB; Q12879; -.
TreeFam; TF314731; -.
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 uopn Ca2+ infux 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.
SignaLink; Q12879; -.
SIGNOR; Q12879; -.
ChiTaRS; GRIN2A; human.
EvolutionaryTrace; Q12879; -.
GeneWiki; GRIN2A; -.
GenomeRNAi; 2903; -.
PRO; PR:Q12879; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000183454; -.
CleanEx; HS_GRIN2A; -.
ExpressionAtlas; Q12879; baseline and differential.
Genevisible; Q12879; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
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; ISS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0022849; F:glutamate-gated calcium ion channel activity; IDA:UniProtKB.
GO; GO:0004972; F:NMDA glutamate receptor activity; ISS:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IDA:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0033058; P:directional locomotion; IEA:Ensembl.
GO; GO:0042417; P:dopamine metabolic process; IEA:Ensembl.
GO; GO:0007215; P:glutamate receptor signaling pathway; TAS:ProtInc.
GO; GO:0007611; P:learning or memory; TAS:ProtInc.
GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0008104; P:protein localization; IEA:Ensembl.
GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IDA:UniProtKB.
GO; GO:0009611; P:response to wounding; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0042428; P:serotonin metabolic process; IEA:Ensembl.
GO; GO:0030431; P:sleep; IEA:Ensembl.
GO; GO:0001964; P:startle response; IEA:Ensembl.
GO; GO:0006810; P:transport; TAS:ProtInc.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
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; Alternative splicing; 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;
Metal-binding; Phosphoprotein; Polymorphism;
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_0000011573.
TOPO_DOM 23 555 Extracellular.
{ECO:0000250|UniProtKB:B7ZSK1}.
TRANSMEM 556 576 Helical. {ECO:0000250|UniProtKB:B7ZSK1}.
TOPO_DOM 577 600 Cytoplasmic.
{ECO:0000250|UniProtKB:B7ZSK1}.
INTRAMEM 601 620 Discontinuously helical.
{ECO:0000250|UniProtKB:B7ZSK1}.
TOPO_DOM 621 625 Cytoplasmic.
{ECO:0000250|UniProtKB:B7ZSK1}.
TRANSMEM 626 645 Helical. {ECO:0000250|UniProtKB:B7ZSK1}.
TOPO_DOM 646 816 Extracellular.
{ECO:0000250|UniProtKB:B7ZSK1}.
TRANSMEM 817 837 Helical. {ECO:0000250|UniProtKB:B7ZSK1}.
TOPO_DOM 838 1464 Cytoplasmic.
{ECO:0000250|UniProtKB:B7ZSK1}.
REGION 511 513 Glutamate binding. {ECO:0000244|PDB:5H8F,
ECO:0000244|PDB:5H8H,
ECO:0000244|PDB:5H8N,
ECO:0000244|PDB:5H8Q,
ECO:0000244|PDB:5I2K,
ECO:0000244|PDB:5I2N,
ECO:0000244|PDB:5KCJ,
ECO:0000244|PDB:5KDT,
ECO:0000244|PDB:5TP9,
ECO:0000244|PDB:5TPA,
ECO:0000269|PubMed:26875626,
ECO:0000269|PubMed:26919761,
ECO:0000269|PubMed:28105280}.
REGION 599 620 Pore-forming.
{ECO:0000250|UniProtKB:B7ZSK1}.
REGION 689 690 Glutamate binding.
{ECO:0000250|UniProtKB:Q00959}.
REGION 730 731 Glutamate binding.
{ECO:0000250|UniProtKB:Q00959}.
MOTIF 1462 1464 PDZ-binding. {ECO:0000305}.
METAL 44 44 Zinc; via tele nitrogen.
{ECO:0000250|UniProtKB:Q00959}.
METAL 128 128 Zinc; via tele nitrogen.
{ECO:0000250|UniProtKB:Q00959}.
METAL 266 266 Zinc. {ECO:0000250|UniProtKB:Q00959}.
METAL 282 282 Zinc. {ECO:0000250|UniProtKB:Q00959}.
BINDING 518 518 Glutamate. {ECO:0000244|PDB:5H8F,
ECO:0000244|PDB:5H8H,
ECO:0000244|PDB:5H8N,
ECO:0000244|PDB:5H8Q,
ECO:0000244|PDB:5I2K,
ECO:0000244|PDB:5I2N,
ECO:0000244|PDB:5KCJ,
ECO:0000244|PDB:5KDT,
ECO:0000244|PDB:5TP9,
ECO:0000244|PDB:5TPA,
ECO:0000269|PubMed:26875626,
ECO:0000269|PubMed:26919761,
ECO:0000269|PubMed:28105280}.
SITE 614 614 Functional determinant of NMDA receptors.
{ECO:0000250}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000250|UniProtKB:P35436}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000250|UniProtKB:P35436}.
MOD_RES 929 929 Phosphoserine.
{ECO:0000250|UniProtKB:P35436}.
MOD_RES 1025 1025 Phosphoserine.
{ECO:0000250|UniProtKB:Q00959}.
MOD_RES 1059 1059 Phosphoserine.
{ECO:0000250|UniProtKB:P35436}.
MOD_RES 1062 1062 Phosphoserine.
{ECO:0000250|UniProtKB:Q00959}.
MOD_RES 1198 1198 Phosphoserine.
{ECO:0000250|UniProtKB:Q00959}.
MOD_RES 1291 1291 Phosphoserine.
{ECO:0000250|UniProtKB:Q00959}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 380 380 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:0000250|UniProtKB:Q00959}.
DISULFID 429 455 {ECO:0000244|PDB:5H8F,
ECO:0000244|PDB:5H8H,
ECO:0000244|PDB:5H8N,
ECO:0000244|PDB:5H8Q,
ECO:0000244|PDB:5I2K,
ECO:0000244|PDB:5I2N,
ECO:0000244|PDB:5KCJ,
ECO:0000244|PDB:5KDT,
ECO:0000244|PDB:5TP9,
ECO:0000244|PDB:5TPA,
ECO:0000269|PubMed:26875626,
ECO:0000269|PubMed:26919761,
ECO:0000269|PubMed:28105280}.
DISULFID 436 456 {ECO:0000244|PDB:5H8F,
ECO:0000244|PDB:5H8H,
ECO:0000244|PDB:5H8N,
ECO:0000244|PDB:5H8Q,
ECO:0000244|PDB:5I2K,
ECO:0000244|PDB:5I2N,
ECO:0000244|PDB:5KCJ,
ECO:0000244|PDB:5KDT,
ECO:0000244|PDB:5TP9,
ECO:0000244|PDB:5TPA,
ECO:0000269|PubMed:26875626,
ECO:0000269|PubMed:26919761,
ECO:0000269|PubMed:28105280}.
DISULFID 745 800 {ECO:0000250|UniProtKB:Q00959}.
VAR_SEQ 1259 1464 NPATGEQVYQQDWAQNNALQLQKNKLRISRQHSYDNIVDKP
RELDLSRPSRSISLKDRERLLEGNFYGSLFSVPSSKLSGKK
SSLFPQGLEDSKRSKSLLPDHTSDNPFLHSHRDDQRLVIGR
CPSDPYKHSLPSQAVNDSYLRSSLRSTASYCSRDSRGHNDV
YISEHVMPYAANKNNMYSTPRVLNSCSNRRVYKKMPSIESD
V -> MTNAWLLGDAPRTLTNTRCHPRR (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_044300.
VARIANT 57 57 P -> L (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067725.
VARIANT 79 79 P -> R (in FESD).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070345.
VARIANT 183 183 F -> I (found in a cutaneous malignant
melanoma sample; somatic mutation; also
found in a patient with benign epilepsy
with centrotemporal spike;
dbSNP:rs587780353).
{ECO:0000269|PubMed:21499247,
ECO:0000269|PubMed:23933819}.
/FTId=VAR_067726.
VARIANT 184 184 I -> S (in FESD; unknown pathological
significance).
{ECO:0000269|PubMed:23933820}.
/FTId=VAR_070346.
VARIANT 231 231 C -> Y (in FESD; unknown pathological
significance).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070347.
VARIANT 243 243 A -> V (in FESD; results in reduced high-
affinity zinc mediated inhibition).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070348.
VARIANT 252 252 D -> N (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs868215122).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067727.
VARIANT 270 270 K -> E. {ECO:0000269|PubMed:8061049}.
/FTId=VAR_010938.
VARIANT 278 278 S -> F (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs148531310).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067728.
VARIANT 290 290 A -> V (in FESD; dbSNP:rs199528312).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070349.
VARIANT 295 295 G -> S (in FESD; unknown pathological
significance; dbSNP:rs568484876).
{ECO:0000269|PubMed:23933820}.
/FTId=VAR_070350.
VARIANT 349 349 S -> F (found in a cutaneous malignant
melanoma sample).
{ECO:0000269|PubMed:24455489}.
/FTId=VAR_071624.
VARIANT 370 370 R -> W (in FESD; dbSNP:rs761168789).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070351.
VARIANT 371 371 E -> K (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs149344082).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067729.
VARIANT 373 373 E -> K (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067730.
VARIANT 380 380 N -> D (found in a patient with neonatal
onset epileptic encephalopathy; unknown
pathological significance).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078109.
VARIANT 436 436 C -> R (in FESD).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070352.
VARIANT 449 449 G -> E (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs139033056).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067731.
VARIANT 459 459 F -> S (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067732.
VARIANT 483 483 G -> R (in FESD; unknown pathological
significance).
{ECO:0000269|PubMed:23933820}.
/FTId=VAR_070353.
VARIANT 504 504 R -> W (in FESD).
{ECO:0000269|PubMed:23933820}.
/FTId=VAR_070354.
VARIANT 518 518 R -> H (in FESD; affects receptor
kinetics; dbSNP:rs397518470).
{ECO:0000269|PubMed:23933820}.
/FTId=VAR_070355.
VARIANT 531 531 T -> M (in FESD; affects receptor
kinetics; dbSNP:rs397518468).
{ECO:0000269|PubMed:23933818}.
/FTId=VAR_070356.
VARIANT 547 547 Missing (in FESD).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070357.
VARIANT 548 548 A -> T (in FESD).
{ECO:0000269|PubMed:23933820}.
/FTId=VAR_070358.
VARIANT 552 552 P -> R (in FESD; dbSNP:rs397518450).
{ECO:0000269|PubMed:23033978}.
/FTId=VAR_069382.
VARIANT 595 595 H -> R (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs551688681).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067733.
VARIANT 598 598 S -> F (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067734.
VARIANT 615 615 N -> K (in FESD; the mutant receptor has
decreased calcium permeability; shows a
dominant-negative effect;
dbSNP:rs397518447).
{ECO:0000269|PubMed:20890276}.
/FTId=VAR_065899.
VARIANT 649 649 L -> V (in FESD; dbSNP:rs397514557).
{ECO:0000269|PubMed:23033978}.
/FTId=VAR_069383.
VARIANT 652 652 F -> V (in FESD; affects receptor
kinetics; dbSNP:rs397518471).
{ECO:0000269|PubMed:23933820}.
/FTId=VAR_070359.
VARIANT 653 653 M -> I (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067735.
VARIANT 669 669 K -> N (in FESD).
{ECO:0000269|PubMed:23933820}.
/FTId=VAR_070360.
VARIANT 694 694 I -> T (in FESD).
{ECO:0000269|PubMed:23933820}.
/FTId=VAR_070361.
VARIANT 699 699 P -> S (in FESD).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070362.
VARIANT 705 705 M -> V (in FESD; unknown pathological
significance).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070363.
VARIANT 712 712 G -> E (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs143031592).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067736.
VARIANT 714 714 E -> K (in FESD).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070364.
VARIANT 716 716 A -> D (in FESD; unknown pathological
significance).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078110.
VARIANT 716 716 A -> T (in FESD; dbSNP:rs762659685).
{ECO:0000269|PubMed:23933820}.
/FTId=VAR_070365.
VARIANT 727 727 A -> T (in FESD).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070366.
VARIANT 731 731 D -> N (in FESD; loss-of-function
characterized by drastically decreased
glutamate agonist potency, decreased
glycine agonist potency, reduced
amplitude of current response, shortened
synaptic-like response time course,
decreased channel open probability and
enhanced sensitivity to negative
allosteric modulators;
dbSNP:rs796052549).
{ECO:0000269|PubMed:23933820,
ECO:0000269|PubMed:28182669}.
/FTId=VAR_070367.
VARIANT 734 734 V -> L (in FESD; unknown pathological
significance).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070368.
VARIANT 740 740 G -> W (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067737.
VARIANT 762 762 G -> A (found in a cutaneous malignant
melanoma sample).
{ECO:0000269|PubMed:24455489}.
/FTId=VAR_071625.
VARIANT 772 772 K -> E (in FESD).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070369.
VARIANT 812 812 L -> M (in FESD; increase in receptor
response to agonists; decrease in the
actions of endogenous negative
modulators; increase in channel open
probability; prolonged deactivation time
course). {ECO:0000269|PubMed:24504326}.
/FTId=VAR_072750.
VARIANT 814 814 I -> T (in FESD; unknown pathological
significance; dbSNP:rs780654733).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070370.
VARIANT 817 817 M -> V (in FESD; gain-of-function
characterized by enhanced agonist
potency, reduced sensitivity to
endogenous negative inhibitors, prolonged
synaptic-like response time course,
increased single-channel mean open time
and increased channel open probability;
dbSNP:rs796052551).
{ECO:0000269|PubMed:24903190,
ECO:0000269|PubMed:28126851}.
/FTId=VAR_071626.
VARIANT 884 884 D -> N (found in a patient with autism;
unknown pathological significance;
dbSNP:rs777684328).
{ECO:0000269|PubMed:26637798}.
/FTId=VAR_078690.
VARIANT 889 889 G -> E (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247,
ECO:0000269|PubMed:24455489}.
/FTId=VAR_067738.
VARIANT 904 904 I -> F (in FESD).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070371.
VARIANT 920 920 R -> K (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067739.
VARIANT 929 929 S -> F (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs767268773).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067740.
VARIANT 933 933 D -> N (in FESD; unknown pathological
significance).
{ECO:0000269|PubMed:23933820}.
/FTId=VAR_070372.
VARIANT 962 962 E -> K (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs765370528).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067741.
VARIANT 976 976 N -> S (in FESD).
{ECO:0000269|PubMed:23933819}.
/FTId=VAR_070373.
VARIANT 989 989 N -> S (found in a patient with neonatal
onset epileptic encephalopathy; unknown
pathological significance;
dbSNP:rs531782747).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078111.
VARIANT 1073 1073 E -> K (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067742.
VARIANT 1074 1074 P -> L (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs867432846).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067743.
VARIANT 1132 1132 P -> L (found in a cutaneous malignant
melanoma sample).
{ECO:0000269|PubMed:24455489}.
/FTId=VAR_071627.
VARIANT 1133 1133 P -> S (found in a cutaneous malignant
melanoma sample).
{ECO:0000269|PubMed:24455489}.
/FTId=VAR_071628.
VARIANT 1153 1153 D -> N (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs267604687).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067744.
VARIANT 1175 1175 E -> K (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs867464241).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067745.
VARIANT 1251 1251 D -> N (in FESD).
{ECO:0000269|PubMed:23933820}.
/FTId=VAR_070374.
VARIANT 1276 1276 A -> G (found in a patient with
continuous spike-wave discharges during
slow-wave sleep; also found in a patient
with drug-resistant focal epilepsy; also
found in a cutaneous malignant melanoma
sample as somatic mutation; unknown
pathological significance;
dbSNP:rs145063086).
{ECO:0000269|PubMed:21499247,
ECO:0000269|PubMed:23933820,
ECO:0000269|PubMed:27864847}.
/FTId=VAR_067746.
VARIANT 1285 1285 R -> K (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs367543132).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067747.
VARIANT 1318 1318 R -> W (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs774419037).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067748.
VARIANT 1366 1366 P -> L (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067749.
VARIANT 1421 1421 D -> N (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067750.
VARIANT 1425 1425 S -> L (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067751.
VARIANT 1426 1426 E -> K (found in a cutaneous malignant
melanoma sample; somatic mutation;
dbSNP:rs138415164).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067752.
VARIANT 1462 1462 S -> C (found in a cutaneous malignant
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21499247}.
/FTId=VAR_067753.
STRAND 405 410 {ECO:0000244|PDB:5H8F}.
TURN 414 416 {ECO:0000244|PDB:5H8F}.
STRAND 417 421 {ECO:0000244|PDB:5H8F}.
TURN 424 426 {ECO:0000244|PDB:5KCJ}.
STRAND 434 442 {ECO:0000244|PDB:5H8F}.
STRAND 449 458 {ECO:0000244|PDB:5H8F}.
HELIX 459 471 {ECO:0000244|PDB:5H8F}.
STRAND 474 479 {ECO:0000244|PDB:5H8F}.
STRAND 482 485 {ECO:0000244|PDB:5H8F}.
STRAND 487 489 {ECO:0000244|PDB:5I2K}.
STRAND 492 494 {ECO:0000244|PDB:5I2K}.
HELIX 495 501 {ECO:0000244|PDB:5H8F}.
STRAND 506 508 {ECO:0000244|PDB:5H8F}.
HELIX 516 519 {ECO:0000244|PDB:5H8F}.
STRAND 522 524 {ECO:0000244|PDB:5H8F}.
STRAND 528 538 {ECO:0000244|PDB:5H8F}.
HELIX 668 671 {ECO:0000244|PDB:5H8F}.
HELIX 673 675 {ECO:0000244|PDB:5H8F}.
STRAND 676 678 {ECO:0000244|PDB:5H8F}.
STRAND 686 688 {ECO:0000244|PDB:5I2K}.
HELIX 689 697 {ECO:0000244|PDB:5H8F}.
HELIX 699 705 {ECO:0000244|PDB:5H8F}.
HELIX 706 708 {ECO:0000244|PDB:5H8F}.
HELIX 713 721 {ECO:0000244|PDB:5H8F}.
STRAND 726 731 {ECO:0000244|PDB:5H8F}.
HELIX 732 740 {ECO:0000244|PDB:5H8F}.
HELIX 743 745 {ECO:0000244|PDB:5I2N}.
STRAND 747 750 {ECO:0000244|PDB:5H8F}.
TURN 751 753 {ECO:0000244|PDB:5H8F}.
STRAND 756 761 {ECO:0000244|PDB:5H8F}.
STRAND 764 766 {ECO:0000244|PDB:5I2K}.
HELIX 772 784 {ECO:0000244|PDB:5H8F}.
HELIX 787 795 {ECO:0000244|PDB:5H8F}.
STRAND 1461 1464 {ECO:0000244|PDB:3NFL}.
SEQUENCE 1464 AA; 165283 MW; AF5EDD599EC0B1E3 CRC64;
MGRVGYWTLL VLPALLVWRG PAPSAAAEKG PPALNIAVML GHSHDVTERE LRTLWGPEQA
AGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF GDDTDQEAVA QMLDFISSHT
FVPILGIHGG ASMIMADKDP TSTFFQFGAS IQQQATVMLK IMQDYDWHVF SLVTTIFPGY
REFISFVKTT VDNSFVGWDM QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL
SEARSLGLTG YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGIGILT
TAASSMLEKF SYIPEAKASC YGQMERPEVP MHTLHPFMVN VTWDGKDLSF TEEGYQVHPR
LVVIVLNKDR EWEKVGKWEN HTLSLRHAVW 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 MHQYMTKFNQ KGVEDALVSL
KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI GSGYIFATTG YGIALQKGSP WKRQIDLALL
QFVGDGEMEE LETLWLTGIC HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL
FYWKLRFCFT GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS
AKNISSMSNM NSSRMDSPKR AADFIQRGSL IMDMVSDKGN LMYSDNRSFQ GKESIFGDNM
NELQTFVANR QKDNLNNYVF QGQHPLTLNE SNPNTVEVAV STESKANSRP RQLWKKSVDS
IRQDSLSQNP VSQRDEATAE NRTHSLKSPR YLPEEMAHSD ISETSNRATC HREPDNSKNH
KTKDNFKRSV ASKYPKDCSE VERTYLKTKS SSPRDKIYTI DGEKEPGFHL DPPQFVENVT
LPENVDFPDP YQDPSENFRK GDSTLPMNRN PLHNEEGLSN NDQYKLYSKH FTLKDKGSPH
SETSERYRQN STHCRSCLSN MPTYSGHFTM RSPFKCDACL RMGNLYDIDE DQMLQETGNP
ATGEQVYQQD WAQNNALQLQ KNKLRISRQH SYDNIVDKPR ELDLSRPSRS ISLKDRERLL
EGNFYGSLFS VPSSKLSGKK SSLFPQGLED SKRSKSLLPD HTSDNPFLHS HRDDQRLVIG
RCPSDPYKHS LPSQAVNDSY LRSSLRSTAS YCSRDSRGHN DVYISEHVMP YAANKNNMYS
TPRVLNSCSN RRVYKKMPSI ESDV


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