GRIN2B
entrez
2904
canonical
uniprot
Q13224
canonical
ensembl
ENSG00000273079
resolver
ensp
ENSP00000477455
resolver
ensp
ENSP00000486677
resolver
enst
ENST00000609686
resolver
enst
ENST00000630791
resolver
genesymbol
GRIN2B
resolver
genesymbol_syn
NMDAR2B
resolver
hgnc
HGNC:4586
resolver
uniprot
A0A8D9PHB2
resolver
uniprot
Q12919
resolver
uniprot
Q13220
resolver
uniprot
Q13225
resolver
uniprot
Q14CU4
resolver
uniprot
Q9UM56
resolver
uniprot_entry
A0A8D9PHB2_HUMAN
resolver
uniprot_entry
NMDE2_HUMAN
resolver
uniprot_sec
Q12919
resolver
uniprot_sec
Q13220
resolver
uniprot_sec
Q13225
resolver
uniprot_sec
Q14CU4
resolver
uniprot_sec
Q9UM56
resolver
amino_acid_sequence
MKPRAECCSPKFWLVLAVLAVSGSRARSQKSPPSIGIAVILVGTSDEVAIKDAHEKDDFHHLSVVPRVELVAMNETDPKSIITRICDLMSDRKIQGVVFADDTDQEAIAQILDFISAQTLTPILGIHGGSSMIMADKDESSMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFVNKIRSTIENSFVGWELEEVLLLDMSLDDGDSKIQNQLKKLQSPIILLYCTKEEATYIFEVANSVGLTGYGYTWIVPSLVAGDTDTVPAEFPTGLISVSYDEWDYGLPARVRDGIAIITTAASDMLSEHSFIPEPKSSCYNTHEKRIYQSNMLNRYLINVTFEGRNLSFSEDGYQMHPKLVIILLNKERKWERVGKWKDKSLQMKYYVWPRMCPETEEQEDDHLSIVTLEEAPFVIVESVDPLSGTCMRNTVPCQKRIVTENKTDEEPGYIKKCCKGFCIDILKKISKSVKFTYDLYLVTNGKHGKKINGTWNGMIGEVVMKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSRSNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYVDQVSGLSDKKFQRPNDFSPPFRFGTVPNGSTERNIRNNYAEMHAYMGKFNQRGVDDALLSLKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLGAAMALSLITFICEHLFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSVMNSPTATMNNTHSNILRLLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSYNNPPCEENLFSDYISEVERTFGNLQLKDSNVYQDHYHHHHRPHSIGSASSIDGLYDCDNPPFTTQSRSISKKPLDIGLPSSKHSQLSDLYGKFSFKSDRYSGHDDLIRSDVSDISTHTVTYGNIEGNAAKRRKQQYKDSLKKRPASAKSRREFDEIELAYRRRPPRSPDHKRYFRDKEGLRDFYLDQFRTKENSPHWEHVDLTDIYKERSDDFKRDSVSGGGPCTNRSHIKHGTGDKHGVVSGVPAPWEKNLTNVEWEDRSGGNFCRSCPSKLHNYSTTVTGQNSGRQACIRCEACKKAGNLYDISEDNSLQELDQPAAPVAVTSNASTTKYPQSPTNSKAQKKNRNKLRRQHSYDTFVDLQKEEAALAPRSVSLKDKGRFMDGSPYAHMFEMSAGESTFANNKSSVPTAGHHHHNNPGGGYMLSKSLYPDRVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVAGASKARPDFRALVTNKPVVSALHGAVPARFQKDICIGNQSNPCVPNNKNPRAFNGSSNGHVYEKLSSIESDV
uniprot
proteins
disease_involvement
DISEASE: Intellectual developmental disorder, autosomal dominant 6, with or without seizures (MRD6) [MIM:613970]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD6 additional features may include seizures, hypotonia, abnormal movements, such as dystonia, and autistic features. {ECO:0000269|PubMed:20890276, ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:23160955, ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:25356899, ECO:0000269|PubMed:27839871, ECO:0000269|PubMed:28095420, ECO:0000269|PubMed:38538865}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Developmental and epileptic encephalopathy 27 (DEE27) [MIM:616139]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. {ECO:0000269|PubMed:24272827, ECO:0000269|PubMed:27839871, ECO:0000269|PubMed:27864847, ECO:0000269|PubMed:38538865}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberrations involving GRIN2B has been found in patients with intellectual disability. Translocations t(9;12)(p23;p13.1) and t(10;12)(q21.1;p13.1) with a common breakpoint in 12p13.1.
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:24272827, PubMed:24863970, PubMed:26875626, PubMed:26919761, PubMed:27839871, PubMed:28095420, PubMed:28126851, PubMed:38538865, PubMed:8768735). Participates in synaptic plasticity for learning and memory formation by contributing to the long-term depression (LTD) of hippocampus membrane currents (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:24272827, PubMed:24863970, PubMed:26875626, PubMed:26919761, PubMed:27839871, PubMed:28095420, PubMed:28126851, PubMed:38538865, 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:28095420, PubMed:28126851, PubMed:38538865, PubMed:8768735). In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (By similarity). {ECO:0000250|UniProtKB:P35438, ECO:0000250|UniProtKB:Q01097, ECO:0000269|PubMed:24272827, ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:27839871, ECO:0000269|PubMed:28095420, ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:38538865, ECO:0000269|PubMed:8768735}.
uniprot
proteins
mass_dalton
166367
uniprot
proteins
mutagenesis
MUTAGEN 553; /note="P->R: Changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency and slowed response rise time and deactivation time course."; /evidence="ECO:0000269|PubMed:28095420"; MUTAGEN 636; /note="A->P: Severely reduced localization to cell membrane."; /evidence="ECO:0000269|PubMed:38538865"; MUTAGEN 636; /note="A->V: Reduced localization to cell membrane. Affects glutamate-gated calcium ion channel activity resulting in increased agonist potency and mutant channels activated at lower glutamate and glycine concentrations."; /evidence="ECO:0000269|PubMed:38538865"; MUTAGEN 639; /note="A->V: Reduced localization to cell membrane. Affects glutamate-gated calcium ion channel activity resulting in increased agonist potency and mutant channels activated at lower glutamate and glycine concentrations."; /evidence="ECO:0000269|PubMed:38538865"; MUTAGEN 641; /note="I->T: Reduced localization to cell membrane. Affects glutamate-gated calcium ion channel activity resulting in increased agonist potency and mutant channels activated at lower glutamate and glycine concentrations."; /evidence="ECO:0000269|PubMed:38538865"; MUTAGEN 649; /note="N->T: Affects glutamate-gated calcium ion channel activity resulting in increased agonist potency and mutant channels activated at lower glutamate and glycine concentrations."; /evidence="ECO:0000269|PubMed:38538865"; MUTAGEN 652; /note="A->G: No significant effect on glutamate and glycine agonist potency."; /evidence="ECO:0000269|PubMed:38538865"; MUTAGEN 655; /note="I->F: Reduced localization to cell membrane."; /evidence="ECO:0000269|PubMed:38538865"; MUTAGEN 818; /note="M->V: Increased glutamate and glycine agonist potency."; /evidence="ECO:0000269|PubMed:28126851
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues (By similarity). Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity (By similarity). {ECO:0000250|UniProtKB:Q00960, ECO:0000250|UniProtKB:Q01097}.
uniprot
proteins
protein_family
Glutamate-gated ion channel (TC 1.A.10.1) family
uniprot
proteins
protein_family
NR2B/GRIN2B subfamily
uniprot
proteins
pubmed
10748157
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
20890276
uniprot
proteins
pubmed
22833210
uniprot
proteins
pubmed
23033978
uniprot
proteins
pubmed
23160955
uniprot
proteins
pubmed
24272827
uniprot
proteins
pubmed
24863970
uniprot
proteins
pubmed
25356899
uniprot
proteins
pubmed
26875626
uniprot
proteins
pubmed
26912815
uniprot
proteins
pubmed
26919761
uniprot
proteins
pubmed
27458189
uniprot
proteins
pubmed
27839871
uniprot
proteins
pubmed
27864847
uniprot
proteins
pubmed
28095420
uniprot
proteins
pubmed
28126851
uniprot
proteins
pubmed
28130356
uniprot
proteins
pubmed
34321660
uniprot
proteins
pubmed
38538865
uniprot
proteins
pubmed
7959773
uniprot
proteins
pubmed
7999784
uniprot
proteins
pubmed
8768735
uniprot
proteins
pubmed
9547169
uniprot
proteins
sequence_length
1484
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:27839871, ECO:0000269|PubMed:28095420, ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:38538865, ECO:0000269|PubMed:8768735}; Multi-pass membrane protein {ECO:0000269|PubMed:34321660}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00960}; Multi-pass membrane protein {ECO:0000269|PubMed:34321660}. Cell projection, dendrite {ECO:0000269|PubMed:27839871}. Late endosome {ECO:0000250|UniProtKB:Q01097}. Lysosome {ECO:0000250|UniProtKB:Q01097}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q01097}. Note=Co-localizes with the motor protein KIF17 along microtubules. {ECO:0000250|UniProtKB:Q01097}.
uniprot
proteins
transmembrane_region
TRANSMEM 556..576; /note="Helical"; /evidence="ECO:0000269|PubMed:34321660, ECO:0007744|PDB:7EU8"; TRANSMEM 628..647; /note="Helical"; /evidence="ECO:0000269|PubMed:34321660, ECO:0007744|PDB:7EU8"; TRANSMEM 820..835; /note="Helical"; /evidence="ECO:0000269|PubMed:34321660, ECO:0007744|PDB:7EU8
uniprot
proteins