Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutamate receptor ionotropic, NMDA 2B

Gene

GRIN2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 Mg2+ (PubMed:8768735, PubMed:26919761, PubMed:26875626, PubMed:28126851). Sensitivity to glutamate and channel kinetics depend on the subunit composition (PubMed:8768735, PubMed:26875626). 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. Contributes to neural pattern formation in the developing brain. Plays a role in long-term depression (LTD) of hippocampus membrane currents and in synaptic plasticity (By similarity).By similarity4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi127ZincBy similarity1
Metal bindingi284ZincBy similarity1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei514GlutamateBy similarity1
Binding sitei519GlutamateBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei615Functional determinant of NMDA receptorsBy similarity1
Binding sitei732GlutamateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport
LigandCalcium, Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-438066 Unblocking of NMDA receptors, glutamate binding and activation
R-HSA-442729 CREB phosphorylation through the activation of CaMKII
R-HSA-442982 Ras activation upon Ca2+ influx through NMDA receptor
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6794361 Neurexins and neuroligins
R-HSA-8849932 Synaptic adhesion-like molecules
R-HSA-9022699 MECP2 regulates neuronal receptors and channels
R-HSA-9032500 Activated NTRK2 signals through FYN

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q13224

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q13224

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glutamate receptor ionotropic, NMDA 2B
Short name:
GluN2B
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-2
N-methyl D-aspartate receptor subtype 2B
Short name:
NMDAR2B1 Publication
Short name:
NR2B
N-methyl-D-aspartate receptor subunit 3
Short name:
NR3
Short name:
hNR31 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GRIN2B
Synonyms:NMDAR2B
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000273079.4

Human Gene Nomenclature Database

More...
HGNCi
HGNC:4586 GRIN2B

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
138252 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q13224

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini27 – 557ExtracellularBy similarityAdd BLAST531
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei558 – 576HelicalBy similarityAdd BLAST19
Topological domaini577 – 603CytoplasmicBy similarityAdd BLAST27
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei604 – 623Discontinuously helicalBy similarityAdd BLAST20
Topological domaini624 – 630CytoplasmicBy similarity7
Transmembranei631 – 646HelicalBy similarityAdd BLAST16
Topological domaini647 – 817ExtracellularBy similarityAdd BLAST171
Transmembranei818 – 837HelicalBy similarityAdd BLAST20
Topological domaini838 – 1484CytoplasmicBy similarityAdd BLAST647

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Mental retardation, autosomal dominant 6, with or without seizures (MRD6)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:613970
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079947413E → G in MRD6; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency. 2 PublicationsCorresponds to variant dbSNP:rs527236034EnsemblClinVar.1
Natural variantiVAR_079948436C → R in MRD6; decreased protein abundance; decreased localization to the cell membrane. 1 Publication1
Natural variantiVAR_076764456C → Y in MRD6; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency and increased open probability. 2 PublicationsCorresponds to variant dbSNP:rs397514555EnsemblClinVar.1
Natural variantiVAR_079949461C → F in MRD6; decreased protein abundance; decreased localization to the cell membrane; decreased glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and increased glycine potency. 1 Publication1
Natural variantiVAR_069384553P → L in MRD6; no effect on localization to the cell membrane; loss of glutamate-gated calcium ion channel activity. 2 PublicationsCorresponds to variant dbSNP:rs397514556EnsemblClinVar.1
Natural variantiVAR_065900682R → C in MRD6; decreased protein abundance; no effect on localization to the cell membrane; no significant effect on calcium ion transmembrane import into cytosol; analysis of agonist dose-response curves for glutamate and glycine are not consistent. 2 PublicationsCorresponds to variant dbSNP:rs387906636EnsemblClinVar.1
Natural variantiVAR_079950696R → H in MRD6; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency. 1 Publication1
Natural variantiVAR_078647820G → E in MRD6. 1 Publication1
Epileptic encephalopathy, early infantile, 27 (EIEE27)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe childhood 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.
See also OMIM:616139
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07823515V → M in EIEE27; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1057519553Ensembl.1
Natural variantiVAR_072663540R → H in EIEE27; decreased protein abundance; decreased localization to the cell membrane; increased glutamate-gated calcium ion channel activity via an allosteric effect which is characterized by increased glutamate and glycine potency and increased open probability; the mutant channel is less sensitive to magnesium inhibition and has increased calcium permeability compared to wild-type. 2 PublicationsCorresponds to variant dbSNP:rs672601378EnsemblClinVar.1
Natural variantiVAR_072664615N → I in EIEE27; severe phenotype with early onset seizures; gain of function mutation; results in neuronal hyperexcitability; the mutant channel is not inhibited by magnesium and has increased calcium permeability compared to wild-type. 1 PublicationCorresponds to variant dbSNP:rs672601377EnsemblClinVar.1
Natural variantiVAR_072665618V → G in EIEE27; severe phenotype with early onset seizures; gain of function mutation; results in neuronal hyperexcitability; the mutant channel is not inhibited by magnesium and has increased calcium permeability compared to wild-type. 1 PublicationCorresponds to variant dbSNP:rs672601376EnsemblClinVar.1
A chromosomal aberrations involving GRIN2B has been found in patients with mental retardation. Translocations t(9;12)(p23;p13.1) and t(10;12)(q21.1;p13.1) with a common breakpoint in 12p13.1.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi553P → R: Changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency and slowed response rise time and deactivation time course. 1 Publication1
Mutagenesisi818M → V: Increased glutamate and glycine agonist potency. 1 Publication1

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

DisGeNET

More...
DisGeNETi
2904

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...
GeneReviewsi
GRIN2B

MalaCards human disease database

More...
MalaCardsi
GRIN2B
MIMi613970 phenotype
616139 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000273079

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
178469 Autosomal dominant non-syndromic intellectual disability
3451 West syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA28980

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1904

Drug and drug target database

More...
DrugBanki
DB00659 Acamprosate
DB06151 Acetylcysteine
DB00289 Atomoxetine
DB00949 Felbamate
DB00996 Gabapentin
DB06741 Gavestinel
DB00502 Haloperidol
DB08954 Ifenprodil
DB06738 Ketobemidone
DB00142 L-Glutamic Acid
DB01043 Memantine
DB04896 Milnacipran
DB00312 Pentobarbital
DB00454 Pethidine
DB01174 Phenobarbital
DB01708 Prasterone
DB00418 Secobarbital
DB01520 Tenocyclidine

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
GRIN2B

Domain mapping of disease mutations (DMDM)

More...
DMDMi
14548162

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 26Sequence analysisAdd BLAST26
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001157727 – 1484Glutamate receptor ionotropic, NMDA 2BAdd BLAST1458

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi74N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi86 ↔ 321By similarity
Glycosylationi341N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi348N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi429 ↔ 456By similarity
Disulfide bondi436 ↔ 457By similarity
Glycosylationi444N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi491N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi542N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi688N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi746 ↔ 801By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei882PhosphoserineBy similarity1
Modified residuei886PhosphoserineBy similarity1
Modified residuei917PhosphoserineBy similarity1
Modified residuei920PhosphoserineBy similarity1
Modified residuei962PhosphotyrosineBy similarity1
Modified residuei1039PhosphotyrosineBy similarity1
Modified residuei1058PhosphoserineBy similarity1
Modified residuei1061PhosphoserineBy similarity1
Modified residuei1064PhosphoserineBy similarity1
Modified residuei1109PhosphotyrosineBy similarity1
Modified residuei1133PhosphotyrosineBy similarity1
Modified residuei1143PhosphoserineBy similarity1
Modified residuei1155PhosphotyrosineBy similarity1
Modified residuei1255PhosphoserineBy similarity1
Modified residuei1259PhosphoserineBy similarity1
Modified residuei1303Phosphoserine; by DAPK1By similarity1
Modified residuei1474PhosphotyrosineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on tyrosine residues (By similarity). Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q13224

PeptideAtlas

More...
PeptideAtlasi
Q13224

PRoteomics IDEntifications database

More...
PRIDEi
Q13224

ProteomicsDB human proteome resource

More...
ProteomicsDBi
59232

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q13224

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q13224

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Primarily found in the fronto-parieto-temporal cortex and hippocampus pyramidal cells, lower expression in the basal ganglia.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000273079 Expressed in 60 organ(s), highest expression level in buccal mucosa cell

CleanEx database of gene expression profiles

More...
CleanExi
HS_GRIN2B

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q13224 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q13224 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA069762

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterotetramer. Forms heterotetrameric channels composed of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A, GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:8768735, PubMed:26919761, PubMed:26875626, PubMed:28126851, PubMed:26912815). Can also form heterotetrameric channels that contain at least one zeta subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B (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).By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
109161, 26 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-285 NMDA receptor complex, GluN1-GluN2B
CPX-294 NMDA receptor complex, GluN1-GluN2A-GluN2B

Database of interacting proteins

More...
DIPi
DIP-41002N

Protein interaction database and analysis system

More...
IntActi
Q13224, 15 interactors

Molecular INTeraction database

More...
MINTi
Q13224

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000279593

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q13224

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11484
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q13224

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q13224

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni604 – 623Pore-formingBy similarityAdd BLAST20
Regioni690 – 691Glutamate bindingBy similarity2
Regioni1292 – 1304Interaction with DAPK1By similarityAdd BLAST13

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1482 – 1484PDZ-bindingBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi984 – 989Poly-His6
Compositional biasi1361 – 1364Poly-His4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1053 Eukaryota
ENOG410XNUR LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155964

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000113802

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG052635

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q13224

KEGG Orthology (KO)

More...
KOi
K05210

Identification of Orthologs from Complete Genome Data

More...
OMAi
RSHLKHG

Database of Orthologous Groups

More...
OrthoDBi
EOG091G09KH

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q13224

TreeFam database of animal gene trees

More...
TreeFami
TF314731

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR019594 Glu/Gly-bd
IPR001508 Iono_rcpt_met
IPR001320 Iontro_rcpt
IPR018884 NMDAR2_C
IPR028082 Peripla_BP_I

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01094 ANF_receptor, 1 hit
PF00060 Lig_chan, 1 hit
PF10613 Lig_chan-Glu_bd, 1 hit
PF10565 NMDAR2_C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00177 NMDARECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00918 Lig_chan-Glu_bd, 1 hit
SM00079 PBPe, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53822 SSF53822, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q13224-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKPRAECCSP KFWLVLAVLA VSGSRARSQK SPPSIGIAVI LVGTSDEVAI
60 70 80 90 100
KDAHEKDDFH HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVFA
110 120 130 140 150
DDTDQEAIAQ ILDFISAQTL TPILGIHGGS SMIMADKDES SMFFQFGPSI
160 170 180 190 200
EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ DFVNKIRSTI ENSFVGWELE
210 220 230 240 250
EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI FEVANSVGLT
260 270 280 290 300
GYGYTWIVPS LVAGDTDTVP AEFPTGLISV SYDEWDYGLP ARVRDGIAII
310 320 330 340 350
TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS
360 370 380 390 400
FSEDGYQMHP KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE
410 420 430 440 450
QEDDHLSIVT LEEAPFVIVE SVDPLSGTCM RNTVPCQKRI VTENKTDEEP
460 470 480 490 500
GYIKKCCKGF CIDILKKISK SVKFTYDLYL VTNGKHGKKI NGTWNGMIGE
510 520 530 540 550
VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR SNGTVSPSAF
560 570 580 590 600
LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF
610 620 630 640 650
TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL
660 670 680 690 700
AAFMIQEEYV DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA
710 720 730 740 750
EMHAYMGKFN QRGVDDALLS LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT
760 770 780 790 800
IGSGKVFAST GYGIAIQKDS GWKRQVDLAI LQLFGDGEME ELEALWLTGI
810 820 830 840 850
CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH LFYWQFRHCF
860 870 880 890 900
MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR
910 920 930 940 950
LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN
960 970 980 990 1000
NPPCEENLFS DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSASSI
1010 1020 1030 1040 1050
DGLYDCDNPP FTTQSRSISK KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS
1060 1070 1080 1090 1100
GHDDLIRSDV SDISTHTVTY GNIEGNAAKR RKQQYKDSLK KRPASAKSRR
1110 1120 1130 1140 1150
EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK ENSPHWEHVD
1160 1170 1180 1190 1200
LTDIYKERSD DFKRDSVSGG GPCTNRSHIK HGTGDKHGVV SGVPAPWEKN
1210 1220 1230 1240 1250
LTNVEWEDRS GGNFCRSCPS KLHNYSTTVT GQNSGRQACI RCEACKKAGN
1260 1270 1280 1290 1300
LYDISEDNSL QELDQPAAPV AVTSNASTTK YPQSPTNSKA QKKNRNKLRR
1310 1320 1330 1340 1350
QHSYDTFVDL QKEEAALAPR SVSLKDKGRF MDGSPYAHMF EMSAGESTFA
1360 1370 1380 1390 1400
NNKSSVPTAG HHHHNNPGGG YMLSKSLYPD RVTQNPFIPT FGDDQCLLHG
1410 1420 1430 1440 1450
SKSYFFRQPT VAGASKARPD FRALVTNKPV VSALHGAVPA RFQKDICIGN
1460 1470 1480
QSNPCVPNNK NPRAFNGSSN GHVYEKLSSI ESDV
Length:1,484
Mass (Da):166,367
Last modified:June 20, 2001 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i40AEB12BE6E50CEF
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0D9SFK0A0A0D9SFK0_HUMAN
Glutamate receptor ionotropic, NMDA...
GRIN2B
35Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1B0GU78A0A1B0GU78_HUMAN
Glutamate receptor ionotropic, NMDA...
GRIN2B
46Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti434V → A in AAD00659 (Ref. 3) Curated1
Sequence conflicti745G → A in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti773K → N in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti773K → N in AAA74930 (PubMed:7959773).Curated1
Sequence conflicti796W → C in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti796W → C in AAA74930 (PubMed:7959773).Curated1
Sequence conflicti888T → P in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti888T → P in AAA74930 (PubMed:7959773).Curated1
Sequence conflicti902L → V in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti902L → V in AAA74930 (PubMed:7959773).Curated1
Sequence conflicti920 – 921SA → RP in AAB60368 (PubMed:7999784).Curated2
Sequence conflicti958L → S in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti958L → S in AAA74930 (PubMed:7959773).Curated1
Sequence conflicti980 – 982VYQ → DHY in AAA69920 (PubMed:7959773).Curated3
Sequence conflicti1056I → M in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti1167V → I in AAB49993 (PubMed:8768735).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07823515V → M in EIEE27; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1057519553Ensembl.1
Natural variantiVAR_07994318V → I1 PublicationCorresponds to variant dbSNP:rs201094029EnsemblClinVar.1
Natural variantiVAR_07994450I → N Found in a patient with schizophrenia; unknown pathological significance. 1 Publication1
Natural variantiVAR_079945271A → V1 PublicationCorresponds to variant dbSNP:rs138098032EnsemblClinVar.1
Natural variantiVAR_079946362L → M Found in a patient with schizophrenia; unknown pathological significance. 1 Publication1
Natural variantiVAR_011317407S → N1 Publication1
Natural variantiVAR_079947413E → G in MRD6; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency. 2 PublicationsCorresponds to variant dbSNP:rs527236034EnsemblClinVar.1
Natural variantiVAR_079948436C → R in MRD6; decreased protein abundance; decreased localization to the cell membrane. 1 Publication1
Natural variantiVAR_076764456C → Y in MRD6; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency and increased open probability. 2 PublicationsCorresponds to variant dbSNP:rs397514555EnsemblClinVar.1
Natural variantiVAR_079949461C → F in MRD6; decreased protein abundance; decreased localization to the cell membrane; decreased glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and increased glycine potency. 1 Publication1
Natural variantiVAR_072663540R → H in EIEE27; decreased protein abundance; decreased localization to the cell membrane; increased glutamate-gated calcium ion channel activity via an allosteric effect which is characterized by increased glutamate and glycine potency and increased open probability; the mutant channel is less sensitive to magnesium inhibition and has increased calcium permeability compared to wild-type. 2 PublicationsCorresponds to variant dbSNP:rs672601378EnsemblClinVar.1
Natural variantiVAR_069384553P → L in MRD6; no effect on localization to the cell membrane; loss of glutamate-gated calcium ion channel activity. 2 PublicationsCorresponds to variant dbSNP:rs397514556EnsemblClinVar.1
Natural variantiVAR_072664615N → I in EIEE27; severe phenotype with early onset seizures; gain of function mutation; results in neuronal hyperexcitability; the mutant channel is not inhibited by magnesium and has increased calcium permeability compared to wild-type. 1 PublicationCorresponds to variant dbSNP:rs672601377EnsemblClinVar.1
Natural variantiVAR_072665618V → G in EIEE27; severe phenotype with early onset seizures; gain of function mutation; results in neuronal hyperexcitability; the mutant channel is not inhibited by magnesium and has increased calcium permeability compared to wild-type. 1 PublicationCorresponds to variant dbSNP:rs672601376EnsemblClinVar.1
Natural variantiVAR_065900682R → C in MRD6; decreased protein abundance; no effect on localization to the cell membrane; no significant effect on calcium ion transmembrane import into cytosol; analysis of agonist dose-response curves for glutamate and glycine are not consistent. 2 PublicationsCorresponds to variant dbSNP:rs387906636EnsemblClinVar.1
Natural variantiVAR_079950696R → H in MRD6; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency. 1 Publication1
Natural variantiVAR_078647820G → E in MRD6. 1 Publication1
Natural variantiVAR_079951825L → V Probable disease-associated mutation found in a patient with autism spectrum disorder. 1 Publication1
Natural variantiVAR_0799521014Q → R Found in a patient with schizophrenia; unknown pathological significance. 1 Publication1
Natural variantiVAR_0799531026G → S1 PublicationCorresponds to variant dbSNP:rs201963596EnsemblClinVar.1
Natural variantiVAR_0799541342M → R1 Publication1
Natural variantiVAR_0799551415S → L Found in a patient with autism spectrum disorder; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs201463390Ensembl.1
Natural variantiVAR_0799561424L → F1 PublicationCorresponds to variant dbSNP:rs748128078Ensembl.1
Natural variantiVAR_0782361439P → A Found in a patient with Landau-Kleffner syndrome; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs758042475EnsemblClinVar.1
Natural variantiVAR_0799571452S → F Found in a patient with schizophrenia; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs756790727EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U90278 mRNA Translation: AAB49993.1
U88963 mRNA Translation: AAD00659.1
U11287 mRNA Translation: AAB60368.1
BC113618 mRNA Translation: AAI13619.1
BC113620 mRNA Translation: AAI13621.1
U28758 mRNA Translation: AAA74930.1
U28861 mRNA Translation: AAA69919.1
U28862 mRNA Translation: AAA69920.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS8662.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I39066
S52086

NCBI Reference Sequences

More...
RefSeqi
NP_000825.2, NM_000834.3
XP_011518930.1, XM_011520628.2
XP_011518931.1, XM_011520629.2
XP_016874708.1, XM_017019219.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.504844
Hs.632856
Hs.654430

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000609686; ENSP00000477455; ENSG00000273079

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2904

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2904

UCSC genome browser

More...
UCSCi
uc001rbt.3 human

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90278 mRNA Translation: AAB49993.1
U88963 mRNA Translation: AAD00659.1
U11287 mRNA Translation: AAB60368.1
BC113618 mRNA Translation: AAI13619.1
BC113620 mRNA Translation: AAI13621.1
U28758 mRNA Translation: AAA74930.1
U28861 mRNA Translation: AAA69919.1
U28862 mRNA Translation: AAA69920.1
CCDSiCCDS8662.1
PIRiI39066
S52086
RefSeqiNP_000825.2, NM_000834.3
XP_011518930.1, XM_011520628.2
XP_011518931.1, XM_011520629.2
XP_016874708.1, XM_017019219.1
UniGeneiHs.504844
Hs.632856
Hs.654430

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S11model-A403-543[»]
B660-801[»]
1S2Smodel-A405-543[»]
B660-801[»]
2IPVmodel-X404-768[»]
5EWJX-ray2.77B/D31-394[»]
5EWLX-ray2.98B/D31-394[»]
5EWMX-ray2.76B/D31-394[»]
ProteinModelPortaliQ13224
SMRiQ13224
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109161, 26 interactors
ComplexPortaliCPX-285 NMDA receptor complex, GluN1-GluN2B
CPX-294 NMDA receptor complex, GluN1-GluN2A-GluN2B
DIPiDIP-41002N
IntActiQ13224, 15 interactors
MINTiQ13224
STRINGi9606.ENSP00000279593

Chemistry databases

BindingDBiQ13224
ChEMBLiCHEMBL1904
DrugBankiDB00659 Acamprosate
DB06151 Acetylcysteine
DB00289 Atomoxetine
DB00949 Felbamate
DB00996 Gabapentin
DB06741 Gavestinel
DB00502 Haloperidol
DB08954 Ifenprodil
DB06738 Ketobemidone
DB00142 L-Glutamic Acid
DB01043 Memantine
DB04896 Milnacipran
DB00312 Pentobarbital
DB00454 Pethidine
DB01174 Phenobarbital
DB01708 Prasterone
DB00418 Secobarbital
DB01520 Tenocyclidine

PTM databases

iPTMnetiQ13224
PhosphoSitePlusiQ13224

Polymorphism and mutation databases

BioMutaiGRIN2B
DMDMi14548162

Proteomic databases

PaxDbiQ13224
PeptideAtlasiQ13224
PRIDEiQ13224
ProteomicsDBi59232

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000609686; ENSP00000477455; ENSG00000273079
GeneIDi2904
KEGGihsa:2904
UCSCiuc001rbt.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2904
DisGeNETi2904
EuPathDBiHostDB:ENSG00000273079.4

GeneCards: human genes, protein and diseases

More...
GeneCardsi
GRIN2B
GeneReviewsiGRIN2B

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0036873
HGNCiHGNC:4586 GRIN2B
HPAiHPA069762
MalaCardsiGRIN2B
MIMi138252 gene
613970 phenotype
616139 phenotype
neXtProtiNX_Q13224
OpenTargetsiENSG00000273079
Orphaneti178469 Autosomal dominant non-syndromic intellectual disability
3451 West syndrome
PharmGKBiPA28980

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1053 Eukaryota
ENOG410XNUR LUCA
GeneTreeiENSGT00940000155964
HOGENOMiHOG000113802
HOVERGENiHBG052635
InParanoidiQ13224
KOiK05210
OMAiRSHLKHG
OrthoDBiEOG091G09KH
PhylomeDBiQ13224
TreeFamiTF314731

Enzyme and pathway databases

ReactomeiR-HSA-3928662 EPHB-mediated forward signaling
R-HSA-438066 Unblocking of NMDA receptors, glutamate binding and activation
R-HSA-442729 CREB phosphorylation through the activation of CaMKII
R-HSA-442982 Ras activation upon Ca2+ influx through NMDA receptor
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6794361 Neurexins and neuroligins
R-HSA-8849932 Synaptic adhesion-like molecules
R-HSA-9022699 MECP2 regulates neuronal receptors and channels
R-HSA-9032500 Activated NTRK2 signals through FYN
SignaLinkiQ13224
SIGNORiQ13224

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
GRIN2B human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
GRIN2B

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
2904

Protein Ontology

More...
PROi
PR:Q13224

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000273079 Expressed in 60 organ(s), highest expression level in buccal mucosa cell
CleanExiHS_GRIN2B
ExpressionAtlasiQ13224 baseline and differential
GenevisibleiQ13224 HS

Family and domain databases

InterProiView protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR019594 Glu/Gly-bd
IPR001508 Iono_rcpt_met
IPR001320 Iontro_rcpt
IPR018884 NMDAR2_C
IPR028082 Peripla_BP_I
PfamiView protein in Pfam
PF01094 ANF_receptor, 1 hit
PF00060 Lig_chan, 1 hit
PF10613 Lig_chan-Glu_bd, 1 hit
PF10565 NMDAR2_C, 1 hit
PRINTSiPR00177 NMDARECEPTOR
SMARTiView protein in SMART
SM00918 Lig_chan-Glu_bd, 1 hit
SM00079 PBPe, 1 hit
SUPFAMiSSF53822 SSF53822, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNMDE2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q13224
Secondary accession number(s): Q12919
, Q13220, Q13225, Q14CU4, Q9UM56
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 20, 2001
Last modified: December 5, 2018
This is version 192 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again