Sequence Detail

ID/Version

Q01097 Q9DCB2 (UniProt | EBI)

Last sequence update: 2001-06-20
Last annotation update: 2025-06-18

Sequence description from provider

RecName: Full=Glutamate receptor ionotropic, NMDA 2B {ECO:0000305}; Short=GluN2B {ECO:0000303|PubMed:26912815};AltName: Full=Glutamate [NMDA] receptor subunit epsilon-2 {ECO:0000303|PubMed:1377365};AltName: Full=N-methyl D-aspartate receptor subty

Provider

SWISS-PROT

Sequence

Polypeptide 1482 aa

Source

Organism mouse

See UniProt | EBI for source

Annotated genes and markers

Follow the symbol links to get more information on the GO terms, expression assays, orthologs, phenotypic alleles, and other information for the genes or markers below.

Type	Symbol	Name	GO Terms	Expression Assays	Orthologs	Phenotypic Alleles
Gene	Grin2b	glutamate receptor, ionotropic, NMDA2B (epsilon 2)	214	123	4	29

Sequence references in MGI

J:1333 Kutsuwada T, et al., Molecular diversity of the NMDA receptor channel [see comments]. Nature. 1992 Jul 2;358(6381):36-41
J:31622 Kutsuwada T, et al., Impairment of suckling response, trigeminal neuronal pattern formation, and hippocampal LTD in NMDA receptor epsilon 2 subunit mutant mice. Neuron. 1996 Feb;16(2):333-44
J:62660 Setou M, et al., Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport. Science. 2000 Jun 9;288(5472):1796-802
J:99680 The FANTOM Consortium and RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group), The Transcriptional Landscape of the Mammalian Genome. Science. 2005;309(5740):1559-1563
J:114130 Matsuda K, et al., Specific assembly with the NMDA receptor 3B subunit controls surface expression and calcium permeability of NMDA receptors. J Neurosci. 2003 Nov 5;23(31):10064-73
J:119798 Metzler M, et al., NMDA receptor function and NMDA receptor-dependent phosphorylation of huntingtin is altered by the endocytic protein HIP1. J Neurosci. 2007 Feb 28;27(9):2298-308
J:145953 Ng D, et al., Neto1 is a novel CUB-domain NMDA receptor-interacting protein required for synaptic plasticity and learning. PLoS Biol. 2009 Feb 24;7(2):e41
J:161179 Tu W, et al., DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage in stroke. Cell. 2010 Jan 22;140(2):222-34
J:187362 Munton RP, et al., Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations. Mol Cell Proteomics. 2007 Feb;6(2):283-93
J:263376 Trinidad JC, et al., Comprehensive identification of phosphorylation sites in postsynaptic density preparations. Mol Cell Proteomics. 2006 May;5(5):914-22
J:282038 Zhang H, et al., TMEM25 modulates neuronal excitability and NMDA receptor subunit NR2B degradation. J Clin Invest. 2019 Sep 3;129(9):3864-3876
J:292518 Huttlin EL, et al., A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89
J:349402 Kaizuka T, et al., FAM81A is a postsynaptic protein that regulates the condensation of postsynaptic proteins via liquid-liquid phase separation. PLoS Biol. 2024 Mar;22(3):e3002006
J:354155 Matsuda K, et al., Cloning and characterization of a novel NMDA receptor subunit NR3B: a dominant subunit that reduces calcium permeability. Brain Res Mol Brain Res. 2002 Apr 30;100(1-2):43-52
J:360498 Matsui T, et al., Functional comparison of D-serine and glycine in rodents: the effect on cloned NMDA receptors and the extracellular concentration. J Neurochem. 1995 Jul;65(1):454-8