NR2A
entrez
2903
canonical
uniprot
Q12879
canonical
ensembl
ENSG00000183454
resolver
ensp
ENSP00000332549
resolver
ensp
ENSP00000379818
resolver
ensp
ENSP00000441572
resolver
ensp
ENSP00000454998
resolver
ensp
ENSP00000502200
resolver
genesymbol
GRIN2A
resolver
genesymbol
NR2A
resolver
genesymbol_syn
GRIN2A
resolver
genesymbol_syn
NMDAR2A
resolver
hgnc
HGNC:4585
resolver
uniprot
O00669
resolver
uniprot
Q17RZ6
resolver
uniprot
Q547U9
resolver
uniprot
Q59EW6
resolver
uniprot_entry
NMDE1_HUMAN
resolver
uniprot_entry
Q547U9_HUMAN
resolver
uniprot_entry
Q59EW6_HUMAN
resolver
uniprot_sec
O00669
resolver
uniprot_sec
Q17RZ6
resolver
activity_regulation
ACTIVITY REGULATION: NMDA glutamate receptor activity is inhibited by endogenous Mg(2+) in a voltage-dependent manner (PubMed:20890276, PubMed:24504326, PubMed:28095420, PubMed:28126851, PubMed:28182669, PubMed:29644724, PubMed:38538865, PubMed:8768735). NMDA glutamate receptor activity is inhibited by endogenous Zn(2+) (PubMed:24504326, PubMed:27288002, PubMed:28126851, PubMed:28182669, PubMed:29644724). NMDA glutamate receptor activity is inhibited by endogenous protons (PubMed:24504326, PubMed:27288002, PubMed:28095420, PubMed:28126851, PubMed:28182669, PubMed:29644724, PubMed:38538865). {ECO:0000269|PubMed:20890276, ECO:0000269|PubMed:24504326, ECO:0000269|PubMed:27288002, ECO:0000269|PubMed:28095420, ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:28182669, ECO:0000269|PubMed:29644724, ECO:0000269|PubMed:38538865, ECO:0000269|PubMed:8768735}.
uniprot
proteins
amino_acid_sequence
MGRVGYWTLLVLPALLVWRGPAPSAAAEKGPPALNIAVMLGHSHDVTERELRTLWGPEQAAGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLVFGDDTDQEAVAQMLDFISSHTFVPILGIHGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDWHVFSLVTTIFPGYREFISFVKTTVDNSFVGWDMQNVITLDTSFEDAKTQVQLKKIHSSVILLYCSKDEAVLILSEARSLGLTGYDFFWIVPSLVSGNTELIPKEFPSGLISVSYDDWDYSLEARVRDGIGILTTAASSMLEKFSYIPEAKASCYGQMERPEVPMHTLHPFMVNVTWDGKDLSFTEEGYQVHPRLVVIVLNKDREWEKVGKWENHTLSLRHAVWPRYKSFSDCEPDDNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNGTVSPSAFLEPFSASVWVMMFVMLLIVSAIAVFVFEYFSPVGYNRNLAKGKAPHGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEFVDQVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHNEKNEVMSSQLDIDNMAGVFYMLAAAMALSLITFIWEHLFYWKLRFCFTGVCSDRPGLLFSISRGIYSCIHGVHIEEKKKSPDFNLTGSQSNMLKLLRSAKNISSMSNMNSSRMDSPKRAADFIQRGSLIMDMVSDKGNLMYSDNRSFQGKESIFGDNMNELQTFVANRQKDNLNNYVFQGQHPLTLNESNPNTVEVAVSTESKANSRPRQLWKKSVDSIRQDSLSQNPVSQRDEATAENRTHSLKSPRYLPEEMAHSDISETSNRATCHREPDNSKNHKTKDNFKRSVASKYPKDCSEVERTYLKTKSSSPRDKIYTIDGEKEPGFHLDPPQFVENVTLPENVDFPDPYQDPSENFRKGDSTLPMNRNPLHNEEGLSNNDQYKLYSKHFTLKDKGSPHSETSERYRQNSTHCRSCLSNMPTYSGHFTMRSPFKCDACLRMGNLYDIDEDQMLQETGNPATGEQVYQQDWAQNNALQLQKNKLRISRQHSYDNIVDKPRELDLSRPSRSISLKDRERLLEGNFYGSLFSVPSSKLSGKKSSLFPQGLEDSKRSKSLLPDHTSDNPFLHSHRDDQRLVIGRCPSDPYKHSLPSQAVNDSYLRSSLRSTASYCSRDSRGHNDVYISEHVMPYAANKNNMYSTPRVLNSCSNRRVYKKMPSIESDV
uniprot
proteins
disease_involvement
DISEASE: Epilepsy, focal, with speech disorder and with or without impaired intellectual development (FESD) [MIM:245570]: An autosomal dominant, highly variable neurologic disorder. Features range from severe early-onset seizures associated with delayed psychomotor development, persistent speech difficulties, and intellectual disability 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, intellectual disability 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:27288002, ECO:0000269|PubMed:27839871, ECO:0000269|PubMed:27864847, ECO:0000269|PubMed:28095420, ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:28182669, ECO:0000269|PubMed:30544257, ECO:0000269|PubMed:38538865}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Rare genetic variations in GRIN2A may be associated with susceptibility to schizophrenia, a severe psychiatric disorder characterized by hallucinations, delusions, disorganized speech and behavior, cognitive impairment, and social withdrawal. {ECO:0000269|PubMed:35396579}.; 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}.
uniprot
proteins
function
FUNCTION: Component of N-methyl-D-aspartate (NMDA) receptors (NMDARs) that function as heterotetrameric, ligand-gated cation channels with high calcium permeability and voltage-dependent block by Mg(2+) (PubMed:20890276, PubMed:23933818, PubMed:23933819, PubMed:23933820, PubMed:24504326, PubMed:26875626, PubMed:26919761, PubMed:28242877, PubMed:36117210, PubMed:38538865, PubMed:8768735). NMDARs participate in synaptic plasticity for learning and memory formation by contributing to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (By similarity). Channel activation requires binding of the neurotransmitter L-glutamate to the GluN2 subunit, glycine or D-serine binding to the GluN1 subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:23933818, PubMed:23933819, PubMed:23933820, PubMed:24504326, PubMed:26875626, PubMed:26919761, PubMed:27288002, PubMed:28095420, PubMed:28105280, PubMed:28126851, PubMed:28182669, PubMed:29644724, PubMed:38307912, PubMed:8768735). NMDARs mediate simultaneously the potassium efflux and the influx of calcium and sodium (By similarity). Each GluN2 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (PubMed:26875626, PubMed:26919761). Participates in the synaptic plasticity regulation through activation by the L-glutamate releaseed by BEST1, into the synaptic cleft, upon F2R/PAR-1 activation in astrocyte (By similarity). {ECO:0000250|UniProtKB:P35436, ECO:0000250|UniProtKB:P35438, ECO:0000269|PubMed:20890276, ECO:0000269|PubMed:23933818, ECO:0000269|PubMed:23933819, ECO:0000269|PubMed:23933820, ECO:0000269|PubMed:24504326, ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:27288002, ECO:0000269|PubMed:28095420, ECO:0000269|PubMed:28105280, ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:28182669, ECO:0000269|PubMed:28242877, ECO:0000269|PubMed:29644724, ECO:0000269|PubMed:36117210, ECO:0000269|PubMed:38307912, ECO:0000269|PubMed:38538865, ECO:0000269|PubMed:8768735}.
uniprot
proteins
mass_dalton
165283
uniprot
proteins
mutagenesis
MUTAGEN 552; /note="P->A: Changed glutamate-gated calcium ion channel activity characterized by increased desensitization."; /evidence="ECO:0000269|PubMed:28095420"; MUTAGEN 552; /note="P->G: Changed glutamate-gated calcium ion channel activity characterized by accelerated response activation time and increased desensitization."; /evidence="ECO:0000269|PubMed:28095420"; MUTAGEN 552; /note="P->I: Changed glutamate-gated calcium ion channel activity characterized by increased desensitization."; /evidence="ECO:0000269|PubMed:28095420"; MUTAGEN 552; /note="P->K: Changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency with delay in rise time and slower deactivation time course."; /evidence="ECO:0000269|PubMed:28095420"; MUTAGEN 552; /note="P->L: No effect on localization to the cell membrane. Changed glutamate-gated calcium ion channel activity characterized by increased desensitization."; /evidence="ECO:0000269|PubMed:28095420"; MUTAGEN 552; /note="P->Q: No effect on localization to the cell membrane. Changed glutamate-gated calcium ion channel activity characterized by decreased response amplitude and changed desensitization without effect on response rise time or deactivation time course."; /evidence="ECO:0000269|PubMed:28095420"; MUTAGEN 632; /note="S->F: No effect on localization to the cell membrane. No effect on agonist potency and channel activation by glutamate and glycine."; /evidence="ECO:0000269|PubMed:38538865"; MUTAGEN 646; /note="T->R: No effect on localization to the cell membrane. Results in increased glycine potency and channel activation at lower agonist concentrations."; /evidence="ECO:0000269|PubMed:38538865
uniprot
proteins
protein_family
Glutamate-gated ion channel (TC 1.A.10.1) family
uniprot
proteins
protein_family
NR2A/GRIN2A subfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
20890276
uniprot
proteins
pubmed
21499247
uniprot
proteins
pubmed
22833210
uniprot
proteins
pubmed
23033978
uniprot
proteins
pubmed
23933818
uniprot
proteins
pubmed
23933819
uniprot
proteins
pubmed
23933820
uniprot
proteins
pubmed
24455489
uniprot
proteins
pubmed
24504326
uniprot
proteins
pubmed
24903190
uniprot
proteins
pubmed
26637798
uniprot
proteins
pubmed
26875626
uniprot
proteins
pubmed
26919761
uniprot
proteins
pubmed
27288002
uniprot
proteins
pubmed
27839871
uniprot
proteins
pubmed
27864847
uniprot
proteins
pubmed
28095420
uniprot
proteins
pubmed
28105280
uniprot
proteins
pubmed
28126851
uniprot
proteins
pubmed
28182669
uniprot
proteins
pubmed
28242877
uniprot
proteins
pubmed
29644724
uniprot
proteins
pubmed
30544257
uniprot
proteins
pubmed
34186027
uniprot
proteins
pubmed
35396579
uniprot
proteins
pubmed
36117210
uniprot
proteins
pubmed
38307912
uniprot
proteins
pubmed
38538865
uniprot
proteins
pubmed
8061049
uniprot
proteins
pubmed
8768735
uniprot
proteins
sequence_length
1464
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q00959}. Cell membrane {ECO:0000269|PubMed:23933820, ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:27839871, ECO:0000269|PubMed:28095420, ECO:0000269|PubMed:28105280, ECO:0000269|PubMed:28242877, ECO:0000269|PubMed:38538865, ECO:0000269|PubMed:8768735}; Multi-pass membrane protein {ECO:0000269|PubMed:34186027}. Synapse {ECO:0000250|UniProtKB:P35436}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00959}; Multi-pass membrane protein {ECO:0000269|PubMed:34186027}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P35436}. Note=Expression at the dendrite cell membrane and at synapses is regulated by SORCS2 and the retromer complex. {ECO:0000250|UniProtKB:P35436}.
uniprot
proteins
transmembrane_region
TRANSMEM 557..576; /note="Helical"; /evidence="ECO:0000269|PubMed:34186027, ECO:0007744|PDB:7EOQ"; TRANSMEM 626..646; /note="Helical"; /evidence="ECO:0000269|PubMed:34186027, ECO:0007744|PDB:7EOQ"; TRANSMEM 815..835; /note="Helical"; /evidence="ECO:0000269|PubMed:34186027, ECO:0007744|PDB:7EOQ
uniprot
proteins