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Details on Person UniProt:Q13224 GRIN2B
| Class:Id | ReferenceGeneProduct:60297 |
|---|---|
| _chainChangeLog | signal peptide:1-26 added on Fri February 6 2015;chain:27-1484 added on Fri February 6 2015 |
| _displayName | UniProt:Q13224 GRIN2B |
| _timestamp | 2026-02-20 21:42:09 |
| chain | signal peptide:1-26 chain:27-1484 |
| checksum | 40AEB12BE6E50CEF |
| comment | 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).CATALYTIC ACTIVITY Ca(2+)(in) = Ca(2+)(out)CATALYTIC ACTIVITY Na(+)(in) = Na(+)(out)CATALYTIC ACTIVITY K(+)(in) = K(+)(out)SUBUNIT Heterotetramer (PubMed:34321660). Forms heterotetrameric channels composed of two GluN1/zeta subunits (GRIN1), and two identical GluN2/epsilon subunits (GRIN2A, GRIN2B, GRIN2C or GRIN2D) or GluN3 subunits (GRIN3A or GRIN3B) (in vitro) (PubMed:26875626, PubMed:26912815, PubMed:26919761, PubMed:28126851, PubMed:34321660, PubMed:8768735). Can also form heterotetrameric channels that contain at least two GluN1 subunits and at least two different GluN2 subunits (or a combination of one GluN2 and one GluN3 subunits) (in vitro) (By similarity). In vivo, the subunit composition may depend on the expression levels of the different subunits (Probable). Found in a complex with GRIN1 and GRIN3B. Found in a complex with GRIN1, GRIN3A and PPP2CB. Interacts with PDZ domains of PATJ, DLG3 and DLG4. Interacts with HIP1 and NETO1 (By similarity). Interacts with MAGI3 (PubMed:10748157). Interacts with DAPK1 (By similarity). Found in a complex with GRIN1 and PRR7 (PubMed:27458189). Interacts with PRR7 (PubMed:27458189). Interacts with CAMK2A (PubMed:28130356). Interacts with ARC; preventing ARC oligomerization (By similarity). Interacts with TMEM25 (By similarity). Interacts (via the extreme C-terminus) with FRMPD2 (via the second PDZ domain); the interaction is direct and is likely to promote NMDAR-mediated neural signal transmission (By similarity). Interacts with FAM81A; the interaction facilitates condensate formation via liquid-liquid phase separation (By similarity).INTERACTION Co-localizes with the motor protein KIF17 along microtubules.TISSUE SPECIFICITY Primarily found in the fronto-parieto-temporal cortex and hippocampus pyramidal cells, lower expression in the basal ganglia.DOMAIN The extracellular N-terminal domain (NTD) endows NMDARs with a unique capacity for allosteric modulation, harboring several binding sites for small molecule ligands that act as subunit-specific allosteric modulators of ion channel activity.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.PTM Phosphorylated on tyrosine residues (By similarity). Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity (By similarity).DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE 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.SIMILARITY Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR2B/GRIN2B subfamily. |
| description | recommendedName: fullName evidence="34"Glutamate receptor ionotropic, NMDA 2B shortName evidence="30"GluN2B alternativeName: Glutamate [NMDA] receptor subunit epsilon-2 alternativeName: N-methyl D-aspartate receptor subtype 2B shortName evidence="31"NMDAR2B shortName: NR2B alternativeName: N-methyl-D-aspartate receptor subunit 3 shortName: NR3 shortName evidence="32"hNR3 |
| geneName | GRIN2B NMDAR2B |
| identifier | Q13224 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Calcium Cell membrane Cell projection Chromosomal rearrangement Cytoplasm Cytoskeleton Disease variant Disulfide bond Endosome Epilepsy Glycoprotein Intellectual disability Ion channel Ion transport Ligand-gated ion channel Lysosome Magnesium Membrane Metal-binding Phosphoprotein Postsynaptic cell membrane Proteomics identification Receptor Reference proteome Signal Synapse Transmembrane Transmembrane helix Transport Zinc |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | GRIN2B |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8989094] ENSEMBL:ENSG00000273079 GRIN2B [Homo sapiens] |
| secondaryIdentifier | NMDE2_HUMAN Q12919 Q13220 Q13225 Q14CU4 Q9UM56 |
| sequenceLength | 1484 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:419558] GRIN2B [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:3928477] p-Y1252,Y1336,Y1474-GRIN2B [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:9032602] p-Y1474-GRIN2B [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:9609765] GRIN2B [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:9610568] GRIN2B [transport vesicle membrane] [Homo sapiens] [EntityWithAccessionedSequence:9612185] p-Y-GRIN2B [plasma membrane] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:3928403] O4'-phospho-L-tyrosine at 1474 [ModifiedResidue:3928444] O4'-phospho-L-tyrosine at 1252 [ModifiedResidue:3928465] O4'-phospho-L-tyrosine at 1336 [ModifiedResidue:9032603] O4'-phospho-L-tyrosine at 1474 [ModifiedResidue:9612180] O4'-phospho-L-tyrosine at unknown position |
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No pathways have been reviewed or authored by UniProt:Q13224 GRIN2B (60297)
