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Glutamate receptor ionotropic, NMDA 1 (GluN1) (Glutamate [NMDA] receptor subunit zeta-1) (N-methyl-D-aspartate receptor subunit NR1) (NMD-R1)

 NMDZ1_HUMAN             Reviewed;         938 AA.
Q05586; A6NLK7; A6NLR1; C9K0X1; P35437; Q12867; Q12868; Q5VSF3;
Q5VSF4; Q5VSF5; Q5VSF6; Q5VSF7; Q5VSF8; Q9UPF8; Q9UPF9;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
31-JAN-2018, entry version 210.
RecName: Full=Glutamate receptor ionotropic, NMDA 1;
Short=GluN1;
AltName: Full=Glutamate [NMDA] receptor subunit zeta-1;
AltName: Full=N-methyl-D-aspartate receptor subunit NR1;
Short=NMD-R1;
Flags: Precursor;
Name=GRIN1; Synonyms=NMDAR1;
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), NUCLEOTIDE SEQUENCE [MRNA] OF
11-938 (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [MRNA] OF 300-938 (ISOFORM
2).
TISSUE=Brain;
PubMed=8406025; DOI=10.1016/0378-1119(93)90309-Q;
Foldes R.L., Rampersad V., Kamboj R.K.;
"Cloning and sequence analysis of cDNAs encoding human hippocampus N-
methyl-D-aspartate receptor subunits: evidence for alternative RNA
splicing.";
Gene 131:293-298(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=7679115;
Karp S.J., Masu M., Eki T., Ozawa K., Nakanishi S.;
"Molecular cloning and chromosomal localization of the key subunit of
the human N-methyl-D-aspartate receptor.";
J. Biol. Chem. 268:3728-3733(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Brain;
PubMed=7685113; DOI=10.1073/pnas.90.11.5057;
Planells-Cases R., Sun W., Ferrer-Montiel A.V., Montal M.;
"Molecular cloning, functional expression, and pharmacological
characterization of an N-methyl-D-aspartate receptor subunit from
human brain.";
Proc. Natl. Acad. Sci. U.S.A. 90:5057-5061(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7622053; DOI=10.1016/0378-1119(95)00044-7;
Zimmer M., Fink T.M., Franke Y., Lichter P., Spiess J.;
"Cloning and structure of the gene encoding the human N-methyl-D-
aspartate receptor (NMDAR1).";
Gene 159:219-223(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7), AND VARIANTS MET-540
AND SER-682.
PubMed=9231706;
Nash N.R., Heilman C.J., Rees H.D., Levey A.I.;
"Cloning and localization of exon 5-containing isoforms of the NMDAR1
subunit in human and rat brains.";
J. Neurochem. 69:485-493(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 332-922 (ISOFORM 4), AND NUCLEOTIDE
SEQUENCE [MRNA] OF 86-259 (ISOFORM 5).
TISSUE=Cerebellum, and Hippocampus;
PubMed=7926821; DOI=10.1016/0378-1119(94)90089-2;
Foldes R.L., Rampersad V., Kamboj R.K.;
"Cloning and sequence analysis of additional splice variants encoding
human N-methyl-D-aspartate receptor (hNR1) subunits.";
Gene 147:303-304(1994).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 364-464 (ISOFORMS 1/2/3).
PubMed=7681588; DOI=10.1073/pnas.90.6.2174;
Younkin D.P., Tang C.-M., Hardy M., Reddy U.R., Shi Q.-Y.,
Pleasure S.J., Lee V.M.-Y., Pleasure D.;
"Inducible expression of neuronal glutamate receptor channels in the
NT2 human cell line.";
Proc. Natl. Acad. Sci. U.S.A. 90:2174-2178(1993).
[9]
PHOSPHORYLATION BY PKC.
PubMed=8316301; DOI=10.1038/364070a0;
Tingley W.G., Roche K.W., Thompson A.K., Huganir R.L.;
"Regulation of NMDA receptor phosphorylation by alternative splicing
of the C-terminal domain.";
Nature 364:70-73(1993).
[10]
INTERACTION WITH MYZAP.
PubMed=18849881; DOI=10.1097/WNR.0b013e328317f05f;
Roginski R.S., Goubaeva F., Mikami M., Fried-Cassorla E., Nair M.R.,
Yang J.;
"GRINL1A colocalizes with N-methyl D-aspartate receptor NR1 subunit
and reduces N-methyl D-aspartate toxicity.";
NeuroReport 19:1721-1726(2008).
[11]
IDENTIFICATION IN A COMPLEX WITH GRIN2B 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).
[12]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF MET-813.
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]
STRUCTURE BY NMR OF 599-621.
PubMed=10201407; DOI=10.1038/7610;
Opella S.J., Marassi F.M., Gesell J.J., Valente A.P., Kim Y.,
Oblatt-Montal M., Montal M.;
"Structures of the M2 channel-lining segments from nicotinic
acetylcholine and NMDA receptors by NMR spectroscopy.";
Nat. Struct. Biol. 6:374-379(1999).
[14] {ECO:0000244|PDB:5I2K, ECO:0000244|PDB:5I2N, ECO:0000244|PDB:5KDT}
X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 394-544 AND 663-800 IN
COMPLEXES WITH GRIN2A AND GLYCINE, 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).
[15] {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 394-544 AND 663-800 IN
COMPLEXES WITH GRIN2A AND GLYCINE, 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).
[16] {ECO:0000244|PDB:5TP9, ECO:0000244|PDB:5TPA}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 394-544 AND 663-800 IN
COMPLEX WITH GRIN2A AND GLYCINE, FUNCTION, SUBCELLULAR LOCATION,
SUBUNIT, 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).
[17]
VARIANTS MRD8 SER-560 INS AND LYS-662, AND CHARACTERIZATION OF
VARIANTS MRD8 SER-560 INS AND LYS-662.
PubMed=21376300; DOI=10.1016/j.ajhg.2011.02.001;
Hamdan F.F., Gauthier J., Araki Y., Lin D.T., Yoshizawa Y.,
Higashi K., Park A.R., Spiegelman D., Dobrzeniecka S., Piton A.,
Tomitori H., Daoud H., Massicotte C., Henrion E., Diallo O.,
Shekarabi M., Marineau C., Shevell M., Maranda B., Mitchell G.,
Nadeau A., D'Anjou G., Vanasse M., Srour M., Lafreniere R.G.,
Drapeau P., Lacaille J.C., Kim E., Lee J.R., Igarashi K.,
Huganir R.L., Rouleau G.A., Michaud J.L.;
"Excess of de novo deleterious mutations in genes associated with
glutamatergic systems in nonsyndromic intellectual disability.";
Am. J. Hum. Genet. 88:306-316(2011).
[18]
VARIANTS GLN-306; SER-349 AND ALA-419.
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).
[19]
VARIANT MRD8 ARG-557.
PubMed=25167861; DOI=10.1136/jmedgenet-2014-102554;
Redin C., Gerard B., Lauer J., Herenger Y., Muller J., Quartier A.,
Masurel-Paulet A., Willems M., Lesca G., El-Chehadeh S., Le Gras S.,
Vicaire S., Philipps M., Dumas M., Geoffroy V., Feger C.,
Haumesser N., Alembik Y., Barth M., Bonneau D., Colin E., Dollfus H.,
Doray B., Delrue M.A., Drouin-Garraud V., Flori E., Fradin M.,
Francannet C., Goldenberg A., Lumbroso S., Mathieu-Dramard M.,
Martin-Coignard D., Lacombe D., Morin G., Polge A., Sukno S.,
Thauvin-Robinet C., Thevenon J., Doco-Fenzy M., Genevieve D.,
Sarda P., Edery P., Isidor B., Jost B., Olivier-Faivre L.,
Mandel J.L., Piton A.;
"Efficient strategy for the molecular diagnosis of intellectual
disability using targeted high-throughput sequencing.";
J. Med. Genet. 51:724-736(2014).
[20]
VARIANTS GLU-552; ILE-641; LYS-650 AND ARG-815.
PubMed=25864721; DOI=10.1111/epi.12987;
Ohba C., Shiina M., Tohyama J., Haginoya K., Lerman-Sagie T.,
Okamoto N., Blumkin L., Lev D., Mukaida S., Nozaki F., Uematsu M.,
Onuma A., Kodera H., Nakashima M., Tsurusaki Y., Miyake N., Tanaka F.,
Kato M., Ogata K., Saitsu H., Matsumoto N.;
"GRIN1 mutations cause encephalopathy with infantile-onset epilepsy,
and hyperkinetic and stereotyped movement disorders.";
Epilepsia 56:841-848(2015).
[21]
VARIANTS MRD8 TRP-217; ARG-557; ARG-618; ARG-620; SER-645; SER-647;
ARG-815; VAL-815; LEU-817; ARG-827 AND CYS-844, VARIANTS GLU-552 AND
556-GLN--SER-938 DEL, CHARACTERIZATION OF VARIANTS MRD8 TRP-217;
556-GLN--SER-938 DEL; ARG-557; ARG-618; ARG-620; SER-645; SER-647;
ARG-815; LEU-817; ARG-827 AND CYS-844, AND CHARACTERIZATION OF VARIANT
556-GLN--SER-938 DEL.
PubMed=27164704; DOI=10.1212/WNL.0000000000002740;
Lemke J.R., Geider K., Helbig K.L., Heyne H.O., Schuetz H.,
Hentschel J., Courage C., Depienne C., Nava C., Heron D.,
Moeller R.S., Hjalgrim H., Lal D., Neubauer B.A., Nuernberg P.,
Thiele H., Kurlemann G., Arnold G.L., Bhambhani V., Bartholdi D.,
Pedurupillay C.R., Misceo D., Frengen E., Stroemme P., Dlugos D.J.,
Doherty E.S., Bijlsma E.K., Ruivenkamp C.A., Hoffer M.J.,
Goldstein A., Rajan D.S., Narayanan V., Ramsey K., Belnap N.,
Schrauwen I., Richholt R., Koeleman B.P., Sa J., Mendonca C.,
de Kovel C.G., Weckhuysen S., Hardies K., De Jonghe P.,
De Meirleir L., Milh M., Badens C., Lebrun M., Busa T., Francannet C.,
Piton A., Riesch E., Biskup S., Vogt H., Dorn T., Helbig I.,
Michaud J.L., Laube B., Syrbe S.;
"Delineating the GRIN1 phenotypic spectrum: A distinct genetic NMDA
receptor encephalopathy.";
Neurology 86:2171-2178(2016).
[22]
VARIANT HIS-227.
PubMed=28051072; DOI=10.1038/ejhg.2016.163;
Rossi M., Chatron N., Labalme A., Ville D., Carneiro M., Edery P.,
des Portes V., Lemke J.R., Sanlaville D., Lesca G.;
"Novel homozygous missense variant of GRIN1 in two sibs with
intellectual disability and autistic features without epilepsy.";
Eur. J. Hum. Genet. 25:376-380(2017).
[23]
VARIANTS MRD8 TYR-688 AND ARG-827.
PubMed=28389307; DOI=10.1016/j.ejmg.2017.04.001;
Zehavi Y., Mandel H., Zehavi A., Rashid M.A., Straussberg R.,
Jabur B., Shaag A., Elpeleg O., Spiegel R.;
"De novo GRIN1 mutations: An emerging cause of severe early infantile
encephalopathy.";
Eur. J. Med. Genet. 60:317-320(2017).
[24]
CHARACTERIZATION OF VARIANT MRD8 ARG-557, AND CHARACTERIZATION OF
VARIANT GLU-552.
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:7685113, PubMed:28126851,
PubMed:26919761, PubMed:26875626, PubMed:28105280). Sensitivity to
glutamate and channel kinetics depend on the subunit composition
(PubMed:26919761). {ECO:0000269|PubMed:26875626,
ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:28105280,
ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:7685113}.
-!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed
of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A,
GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:7685113,
PubMed:28126851, PubMed:26919761, PubMed:26875626,
PubMed:28105280). Can also form heterotetrameric channels that
contain at least one zeta subunit (GRIN1), an epsilon subunit,
plus GRIN3A or GRIN3B (in vitro). In vivo, the subunit composition
may vary in function of the expression levels of the different
subunits. Found in a complex with GRIN2A or GRIN2B, GRIN3A and
PPP2CB (By similarity). Found in a complex with GRIN2A or GRIN2B
and GRIN3B (By similarity). Interacts with SNX27 (via PDZ domain);
the interaction is required for recycling to the plasma membrane
when endocytosed and prevent degradation in lysosomes (By
similarity). Interacts with DLG4 and MPDZ. Interacts with LRFN1
and LRFN2 (By similarity). Interacts with MYZAP (PubMed:18849881).
Found in a complex with DLG4 and PRR7 (By similarity). Found in a
complex with GRIN2B and PRR7 (PubMed:27458189). Interacts with
PRR7; the interaction is reduced following NMDA receptor activity
(PubMed:27458189). {ECO:0000250|UniProtKB:P35438,
ECO:0000250|UniProtKB:P35439, ECO:0000269|PubMed:18849881,
ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:26919761,
ECO:0000269|PubMed:27458189, ECO:0000269|PubMed:28105280,
ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:7685113}.
-!- INTERACTION:
Q62936:Dlg3 (xeno); NbExp=3; IntAct=EBI-8286218, EBI-349596;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26875626,
ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:28105280,
ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:7685113}; Multi-
pass membrane protein {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density {ECO:0000250}.
Note=Enriched in postsynaptic plasma membrane and postsynaptic
densities. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=3; Synonyms=Long, NR1-3;
IsoId=Q05586-1; Sequence=Displayed;
Name=1; Synonyms=Short, NR1-1;
IsoId=Q05586-2; Sequence=VSP_000137, VSP_000138;
Name=2; Synonyms=Medium, NR1-2;
IsoId=Q05586-3; Sequence=VSP_000139;
Name=4;
IsoId=Q05586-4; Sequence=VSP_011778, VSP_011779;
Name=5;
IsoId=Q05586-5; Sequence=VSP_011777;
Name=6;
IsoId=Q05586-6; Sequence=VSP_011777, VSP_011778, VSP_011779;
Name=7;
IsoId=Q05586-7; Sequence=VSP_011777, VSP_045464;
-!- 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:A0A1L8F5J9}.
-!- PTM: NMDA is probably regulated by C-terminal phosphorylation of
an isoform of NR1 by PKC. Dephosphorylated on Ser-897 probably by
protein phosphatase 2A (PPP2CB). Its phosphorylated state is
influenced by the formation of the NMDAR-PPP2CB complex and the
NMDAR channel activity. {ECO:0000269|PubMed:8316301}.
-!- DISEASE: Mental retardation, autosomal dominant 8 (MRD8)
[MIM:614254]: A disorder characterized by significantly below
average general intellectual functioning associated with
impairments in adaptive behavior and manifested during the
developmental period. {ECO:0000269|PubMed:21376300,
ECO:0000269|PubMed:25167861, ECO:0000269|PubMed:27164704,
ECO:0000269|PubMed:28095420, ECO:0000269|PubMed:28389307}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR1/GRIN1 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=NMDA receptor entry;
URL="https://en.wikipedia.org/wiki/NMDA_receptor";
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EMBL; L13266; AAB59360.1; -; mRNA.
EMBL; L13267; AAA36198.1; -; mRNA.
EMBL; L13268; AAB59361.1; -; mRNA.
EMBL; D13515; BAA02732.1; -; mRNA.
EMBL; L05666; AAA21180.1; -; mRNA.
EMBL; AF015730; AAB67723.1; -; mRNA.
EMBL; AF015731; AAB67724.1; -; mRNA.
EMBL; Z32772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z32773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z32774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL929554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U08106; AAA62111.1; -; mRNA.
EMBL; U08107; AAA62112.1; -; mRNA.
EMBL; S57708; AAB25917.1; -; mRNA.
CCDS; CCDS43910.1; -. [Q05586-2]
CCDS; CCDS55354.1; -. [Q05586-6]
CCDS; CCDS55355.1; -. [Q05586-7]
CCDS; CCDS7031.1; -. [Q05586-1]
CCDS; CCDS7032.1; -. [Q05586-3]
PIR; A46612; A46612.
PIR; A47551; A47551.
RefSeq; NP_000823.4; NM_000832.6. [Q05586-2]
RefSeq; NP_001172019.1; NM_001185090.1. [Q05586-6]
RefSeq; NP_001172020.1; NM_001185091.1. [Q05586-7]
RefSeq; NP_015566.1; NM_007327.3. [Q05586-1]
RefSeq; NP_067544.1; NM_021569.3. [Q05586-3]
RefSeq; XP_005266128.1; XM_005266071.3. [Q05586-4]
RefSeq; XP_005266130.1; XM_005266073.4. [Q05586-5]
UniGene; Hs.558334; -.
PDB; 2HQW; X-ray; 1.90 A; B=875-898.
PDB; 2NR1; NMR; -; A=599-621.
PDB; 3BYA; X-ray; 1.85 A; B=875-898.
PDB; 5H8F; X-ray; 1.81 A; B=394-544, B=663-800.
PDB; 5H8H; X-ray; 2.23 A; B=394-544, B=663-800.
PDB; 5H8N; X-ray; 2.50 A; B=394-544, B=663-800.
PDB; 5H8Q; X-ray; 1.90 A; B=394-544, B=663-800.
PDB; 5I2K; X-ray; 2.86 A; B=394-544, B=663-800.
PDB; 5I2N; X-ray; 2.12 A; B=394-544, B=663-800.
PDB; 5KCJ; X-ray; 2.09 A; B=394-544, B=663-800.
PDB; 5KDT; X-ray; 2.44 A; B=394-544, B=663-800.
PDB; 5TP9; X-ray; 2.40 A; B=394-544, B=663-800.
PDB; 5TPA; X-ray; 2.48 A; B=394-544, B=663-800.
PDBsum; 2HQW; -.
PDBsum; 2NR1; -.
PDBsum; 3BYA; -.
PDBsum; 5H8F; -.
PDBsum; 5H8H; -.
PDBsum; 5H8N; -.
PDBsum; 5H8Q; -.
PDBsum; 5I2K; -.
PDBsum; 5I2N; -.
PDBsum; 5KCJ; -.
PDBsum; 5KDT; -.
PDBsum; 5TP9; -.
PDBsum; 5TPA; -.
ProteinModelPortal; Q05586; -.
SMR; Q05586; -.
BioGrid; 109159; 11.
CORUM; Q05586; -.
IntAct; Q05586; 7.
MINT; MINT-1900224; -.
STRING; 9606.ENSP00000360608; -.
BindingDB; Q05586; -.
ChEMBL; CHEMBL2015; -.
DrugBank; DB00659; Acamprosate.
DrugBank; DB06151; Acetylcysteine.
DrugBank; DB08838; Agmatine.
DrugBank; DB00289; Atomoxetine.
DrugBank; DB05824; CNS-5161.
DrugBank; DB04620; Cycloleucine.
DrugBank; DB03929; D-Serine.
DrugBank; DB00996; Gabapentin.
DrugBank; DB06741; Gavestinel.
DrugBank; DB08954; Ifenprodil.
DrugBank; DB06738; Ketobemidone.
DrugBank; DB00142; L-Glutamic Acid.
DrugBank; DB01043; Memantine.
DrugBank; DB04896; Milnacipran.
DrugBank; DB01173; Orphenadrine.
DrugBank; DB00312; Pentobarbital.
DrugBank; DB00454; Pethidine.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB01708; Prasterone.
DrugBank; DB00418; Secobarbital.
GuidetoPHARMACOLOGY; 455; -.
TCDB; 1.A.10.1.20; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
iPTMnet; Q05586; -.
PhosphoSitePlus; Q05586; -.
BioMuta; GRIN1; -.
DMDM; 548377; -.
PaxDb; Q05586; -.
PeptideAtlas; Q05586; -.
PRIDE; Q05586; -.
Ensembl; ENST00000371546; ENSP00000360601; ENSG00000176884. [Q05586-5]
Ensembl; ENST00000371550; ENSP00000360605; ENSG00000176884. [Q05586-3]
Ensembl; ENST00000371553; ENSP00000360608; ENSG00000176884. [Q05586-6]
Ensembl; ENST00000371559; ENSP00000360614; ENSG00000176884. [Q05586-2]
Ensembl; ENST00000371560; ENSP00000360615; ENSG00000176884. [Q05586-7]
Ensembl; ENST00000371561; ENSP00000360616; ENSG00000176884. [Q05586-1]
GeneID; 2902; -.
KEGG; hsa:2902; -.
UCSC; uc004clk.4; human. [Q05586-1]
CTD; 2902; -.
DisGeNET; 2902; -.
EuPathDB; HostDB:ENSG00000176884.14; -.
GeneCards; GRIN1; -.
HGNC; HGNC:4584; GRIN1.
HPA; CAB006831; -.
MalaCards; GRIN1; -.
MIM; 138249; gene.
MIM; 614254; phenotype.
neXtProt; NX_Q05586; -.
OpenTargets; ENSG00000176884; -.
Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
PharmGKB; PA28978; -.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
GeneTree; ENSGT00760000119186; -.
HOGENOM; HOG000231491; -.
HOVERGEN; HBG052638; -.
InParanoid; Q05586; -.
KO; K05208; -.
OMA; SGFYHIP; -.
OrthoDB; EOG091G0M5H; -.
PhylomeDB; Q05586; -.
TreeFam; TF351405; -.
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 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; Q05586; -.
ChiTaRS; GRIN1; human.
EvolutionaryTrace; Q05586; -.
GeneWiki; GRIN1; -.
GenomeRNAi; 2902; -.
PMAP-CutDB; Q5VSF3; -.
PRO; PR:Q05586; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000176884; -.
CleanEx; HS_GRIN1; -.
ExpressionAtlas; Q05586; baseline and differential.
Genevisible; Q05586; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0060076; C:excitatory synapse; ISS:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS: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; ISS:UniProtKB.
GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0043083; C:synaptic cleft; ISS:BHF-UCL.
GO; GO:0097060; C:synaptic membrane; ISS:ARUK-UCL.
GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
GO; GO:0043195; C:terminal bouton; ISS:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0016595; F:glutamate binding; IDA:UniProtKB.
GO; GO:0022849; F:glutamate-gated calcium ion channel activity; IDA:UniProtKB.
GO; GO:0016594; F:glycine binding; IDA:UniProtKB.
GO; GO:0042165; F:neurotransmitter binding; ISS:BHF-UCL.
GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; ISS:ARUK-UCL.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl.
GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
GO; GO:0055074; P:calcium ion homeostasis; ISS:UniProtKB.
GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IDA:UniProtKB.
GO; GO:0006812; P:cation transport; IDA:UniProtKB.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0001661; P:conditioned taste aversion; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0060079; P:excitatory postsynaptic potential; ISS:UniProtKB.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007616; P:long-term memory; IEA:Ensembl.
GO; GO:0060179; P:male mating behavior; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0008355; P:olfactory learning; IEA:Ensembl.
GO; GO:0021586; P:pons maturation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISS:ARUK-UCL.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISS:ARUK-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
GO; GO:0018964; P:propylene metabolic process; ISS:BHF-UCL.
GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
GO; GO:0050770; P:regulation of axonogenesis; IEA:Ensembl.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IEA:Ensembl.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0042391; P:regulation of membrane potential; IDA:UniProtKB.
GO; GO:0043576; P:regulation of respiratory gaseous exchange; IEA:Ensembl.
GO; GO:0051963; P:regulation of synapse assembly; IEA:Ensembl.
GO; GO:0007585; P:respiratory gaseous exchange; IEA:Ensembl.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IDA:UniProtKB.
GO; GO:1905429; P:response to glycine; IDA:UniProtKB.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0035176; P:social behavior; IEA:Ensembl.
GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0008542; P:visual learning; ISS:UniProtKB.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR018882; CaM-bd_C0_NMDA_rcpt_NR1.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF10562; CaM_bdg_C0; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 1.
PRINTS; PR00177; NMDARECEPTOR.
SMART; SM00918; Lig_chan-Glu_bd; 1.
SMART; SM00079; PBPe; 1.
SUPFAM; SSF53822; SSF53822; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell junction;
Cell membrane; Complete proteome; Disease mutation; Disulfide bond;
Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
Magnesium; Membrane; Mental retardation; Phosphoprotein; Polymorphism;
Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
Synapse; Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 938 Glutamate receptor ionotropic, NMDA 1.
/FTId=PRO_0000011587.
TOPO_DOM 19 559 Extracellular.
{ECO:0000250|UniProtKB:P35439}.
TRANSMEM 560 580 Helical. {ECO:0000250|UniProtKB:P35439}.
TOPO_DOM 581 602 Cytoplasmic.
{ECO:0000250|UniProtKB:P35439}.
INTRAMEM 603 624 Discontinuously helical.
{ECO:0000250|UniProtKB:A0A1L8F5J9}.
TOPO_DOM 625 630 Cytoplasmic.
{ECO:0000250|UniProtKB:P35439}.
TRANSMEM 631 647 Helical. {ECO:0000250|UniProtKB:P35439}.
TOPO_DOM 648 812 Extracellular.
{ECO:0000250|UniProtKB:P35439}.
TRANSMEM 813 833 Helical. {ECO:0000250|UniProtKB:P35439}.
TOPO_DOM 834 938 Cytoplasmic.
{ECO:0000250|UniProtKB:P35439}.
REGION 516 518 Glycine 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 603 624 Pore-forming.
{ECO:0000250|UniProtKB:A0A1L8F5J9}.
BINDING 523 523 Glycine. {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}.
BINDING 688 688 Glycine. {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}.
BINDING 732 732 Glycine. {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}.
MOD_RES 889 889 Phosphoserine; by PKC.
{ECO:0000305|PubMed:8316301}.
MOD_RES 890 890 Phosphoserine; by PKC.
{ECO:0000305|PubMed:8316301}.
MOD_RES 896 896 Phosphoserine; by PKC.
{ECO:0000305|PubMed:8316301}.
MOD_RES 897 897 Phosphoserine; by PKC.
{ECO:0000305|PubMed:8316301}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 203 203 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 471 471 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 79 308 {ECO:0000250|UniProtKB:P35439}.
DISULFID 420 454 {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 436 455 {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 744 798 {ECO:0000244|PDB:5H8F,
ECO:0000244|PDB:5I2K,
ECO:0000244|PDB:5TPA,
ECO:0000269|PubMed:26875626,
ECO:0000269|PubMed:26919761,
ECO:0000269|PubMed:28105280}.
VAR_SEQ 190 190 K -> KSKKRNYENLDQLSYDNKRGPK (in isoform
5, isoform 6 and isoform 7).
{ECO:0000303|PubMed:7926821,
ECO:0000303|PubMed:9231706}.
/FTId=VSP_011777.
VAR_SEQ 864 938 DRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDTSTGG
GRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES -> QYH
PTDITGPLNLSDPSVSTVV (in isoform 7).
{ECO:0000303|PubMed:9231706}.
/FTId=VSP_045464.
VAR_SEQ 864 900 Missing (in isoform 2).
{ECO:0000303|PubMed:8406025}.
/FTId=VSP_000139.
VAR_SEQ 864 885 DRKSGRAEPDPKKKATFRAITS -> QYHPTDITGPLNLSD
PSVSTVV (in isoform 1).
{ECO:0000303|PubMed:7685113,
ECO:0000303|PubMed:8406025}.
/FTId=VSP_000137.
VAR_SEQ 886 938 Missing (in isoform 1).
{ECO:0000303|PubMed:7685113,
ECO:0000303|PubMed:8406025}.
/FTId=VSP_000138.
VAR_SEQ 901 922 STGGGRGALQNQKDTVLPRRAI -> QYHPTDITGPLNLSD
PSVSTVV (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:7926821,
ECO:0000303|PubMed:9231706}.
/FTId=VSP_011778.
VAR_SEQ 923 938 Missing (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:7926821,
ECO:0000303|PubMed:9231706}.
/FTId=VSP_011779.
VARIANT 217 217 R -> W (in MRD8; changed glutamate-gated
calcium ion channel activity; increased
inhibition by zinc).
{ECO:0000269|PubMed:27164704}.
/FTId=VAR_079984.
VARIANT 227 227 D -> H (found in patients with
intellectual disability and autistic
features; unknown pathological
significance; dbSNP:rs869312865).
{ECO:0000269|PubMed:28051072}.
/FTId=VAR_079985.
VARIANT 306 306 R -> Q (found in a patient with
schizophrenia; unknown pathological
significance).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079986.
VARIANT 349 349 A -> S (in dbSNP:rs148008303).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079987.
VARIANT 419 419 T -> A (in dbSNP:rs763133592).
{ECO:0000269|PubMed:22833210}.
/FTId=VAR_079988.
VARIANT 540 540 I -> M (in dbSNP:rs3181457).
{ECO:0000269|PubMed:9231706}.
/FTId=VAR_049187.
VARIANT 552 552 D -> E (found in a patient with early
onset epileptic encephalopathy; changed
localization to the cell membrane;
decreased glutamate-gated calcium ion
channel activity).
{ECO:0000269|PubMed:25864721,
ECO:0000269|PubMed:27164704,
ECO:0000269|PubMed:28095420}.
/FTId=VAR_079989.
VARIANT 556 938 Missing (found in a patient with fatal
epileptic encephalopathy; loss of
function in calcium ion transmembrane
import into cytosol).
{ECO:0000269|PubMed:27164704}.
/FTId=VAR_079990.
VARIANT 557 557 P -> R (in MRD8; changed localization to
the cell membrane; loss of glutamate-
gated calcium ion channel activity;
dbSNP:rs878853143).
{ECO:0000269|PubMed:25167861,
ECO:0000269|PubMed:27164704,
ECO:0000269|PubMed:28095420}.
/FTId=VAR_079991.
VARIANT 560 560 S -> SS (in MRD8; there is near abolition
of the activity of the NMDA receptor in
Xenopus oocytes; alters the 3-dimensional
structure at the receptor's channel pore
entrance). {ECO:0000269|PubMed:21376300}.
/FTId=VAR_066597.
VARIANT 618 618 G -> R (in MRD8; loss of function in
calcium ion transmembrane import into
cytosol). {ECO:0000269|PubMed:27164704}.
/FTId=VAR_079992.
VARIANT 620 620 G -> R (in MRD8; loss of function in
calcium ion transmembrane import into
cytosol; dbSNP:rs797045047).
{ECO:0000269|PubMed:27164704}.
/FTId=VAR_079993.
VARIANT 641 641 M -> I (found in a patient with early
onset epileptic encephalopathy; unknown
pathological significance).
{ECO:0000269|PubMed:25864721}.
/FTId=VAR_079994.
VARIANT 645 645 A -> S (in MRD8; unknown pathological
significance; no effect on glutamate-
gated calcium ion channel activity).
{ECO:0000269|PubMed:27164704}.
/FTId=VAR_079995.
VARIANT 647 647 Y -> S (in MRD8; loss of glutamate-gated
calcium ion channel activity).
{ECO:0000269|PubMed:27164704}.
/FTId=VAR_079996.
VARIANT 650 650 N -> K (found in a patient with early
onset epileptic encephalopathy; unknown
pathological significance).
{ECO:0000269|PubMed:25864721}.
/FTId=VAR_079997.
VARIANT 662 662 E -> K (in MRD8; this mutation produces a
significant increase in NMDA receptor-
induced calcium currents; excessive
calcium influx through NMDA receptor
could lead to excitotoxic neuronal cell
damage; dbSNP:rs387906635).
{ECO:0000269|PubMed:21376300}.
/FTId=VAR_066598.
VARIANT 682 682 A -> S (in dbSNP:rs1126448).
{ECO:0000269|PubMed:9231706}.
/FTId=VAR_069057.
VARIANT 688 688 S -> Y (in MRD8).
{ECO:0000269|PubMed:28389307}.
/FTId=VAR_079998.
VARIANT 815 815 G -> R (in MRD8; also found in a patient
with early onset epileptic
encephalopathy; loss of glutamate-gated
calcium ion channel activity;
dbSNP:rs797044925).
{ECO:0000269|PubMed:25864721,
ECO:0000269|PubMed:27164704}.
/FTId=VAR_079999.
VARIANT 815 815 G -> V (in MRD8).
{ECO:0000269|PubMed:27164704}.
/FTId=VAR_080000.
VARIANT 817 817 F -> L (in MRD8; decreased glutamate-
gated calcium ion channel activity).
{ECO:0000269|PubMed:27164704}.
/FTId=VAR_080001.
VARIANT 827 827 G -> R (in MRD8; loss of function in
calcium ion transmembrane import into
cytosol). {ECO:0000269|PubMed:27164704,
ECO:0000269|PubMed:28389307}.
/FTId=VAR_080002.
VARIANT 844 844 R -> C (in MRD8; no effect on glutamate-
gated calcium ion channel activity).
{ECO:0000269|PubMed:27164704}.
/FTId=VAR_080003.
MUTAGEN 813 813 M->V: Slight decrease in glycine agonist
potency; no effect on glutamate agonist
potency. {ECO:0000269|PubMed:28126851}.
CONFLICT 389 389 P -> S (in Ref. 8; AAB25917).
{ECO:0000305}.
CONFLICT 488 488 E -> K (in Ref. 1; AAB59361).
{ECO:0000305}.
STRAND 398 402 {ECO:0000244|PDB:5H8F}.
TURN 406 408 {ECO:0000244|PDB:5H8F}.
STRAND 409 413 {ECO:0000244|PDB:5H8F}.
STRAND 426 428 {ECO:0000244|PDB:5I2K}.
STRAND 434 441 {ECO:0000244|PDB:5H8F}.
STRAND 450 457 {ECO:0000244|PDB:5H8F}.
HELIX 458 470 {ECO:0000244|PDB:5H8F}.
STRAND 474 478 {ECO:0000244|PDB:5H8F}.
STRAND 487 489 {ECO:0000244|PDB:5H8F}.
STRAND 496 498 {ECO:0000244|PDB:5H8F}.
HELIX 500 506 {ECO:0000244|PDB:5H8F}.
STRAND 511 513 {ECO:0000244|PDB:5H8F}.
HELIX 521 524 {ECO:0000244|PDB:5H8F}.
STRAND 527 529 {ECO:0000244|PDB:5H8F}.
STRAND 533 543 {ECO:0000244|PDB:5H8F}.
HELIX 600 620 {ECO:0000244|PDB:2NR1}.
HELIX 670 673 {ECO:0000244|PDB:5H8F}.
STRAND 677 679 {ECO:0000244|PDB:5I2N}.
HELIX 688 695 {ECO:0000244|PDB:5H8F}.
HELIX 697 699 {ECO:0000244|PDB:5H8F}.
HELIX 700 707 {ECO:0000244|PDB:5H8F}.
STRAND 711 713 {ECO:0000244|PDB:5H8F}.
HELIX 714 722 {ECO:0000244|PDB:5H8F}.
STRAND 727 732 {ECO:0000244|PDB:5H8F}.
HELIX 733 742 {ECO:0000244|PDB:5H8F}.
STRAND 746 758 {ECO:0000244|PDB:5H8F}.
STRAND 761 763 {ECO:0000244|PDB:5H8Q}.
HELIX 769 781 {ECO:0000244|PDB:5H8F}.
HELIX 784 792 {ECO:0000244|PDB:5H8F}.
HELIX 877 892 {ECO:0000244|PDB:3BYA}.
SEQUENCE 938 AA; 105373 MW; CDF5402769E530AB CRC64;
MSTMRLLTLA LLFSCSVARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL
NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG
LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYSW NHIILLVSDD HEGRAAQKRL
ETLLEERESK AEKVLQFDPG TKNVTALLME AKELEARVII LSASEDDAAT VYRAAAMLNM
TGSGYVWLVG EREISGNALR YAPDGILGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN
ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN YSIMNLQNRK
LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI VTIHQEPFVY VKPTLSDGTC
KEEFTVNGDP VKKVICTGPN DTSPGSPRHT VPQCCYGFCI DLLIKLARTM NFTYEVHLVA
DGKFGTQERV NNSNKKEWNG MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI
LVKKEIPRST LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA
LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN LAAFLVLDRP
EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS TMYRHMEKHN YESAAEAIQA
VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH
ENGFMEDLDK TWVRYQECDS RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH
KDARRKQMQL AFAAVNVWRK NLQDRKSGRA EPDPKKKATF RAITSTLASS FKRRRSSKDT
STGGGRGALQ NQKDTVLPRR AIEREEGQLQ LCSRHRES


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