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UniProtKB - Q12879 (NMDE1_HUMAN)

Entry version 215 (07 Apr 2021)
Sequence version 1 (01 Nov 1996)
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Protein

Glutamate receptor ionotropic, NMDA 2A

Gene

GRIN2A

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:28105280). Sensitivity to glutamate and channel kinetics depend on the subunit composition; channels containing GRIN1 and GRIN2A have lower sensitivity to glutamate and faster deactivation kinetics than channels formed by GRIN1 and GRIN2B (PubMed:26919761, PubMed:26875626). Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (By similarity).By similarity4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi44Zinc; via tele nitrogenBy similarity1
Metal bindingi128Zinc; via tele nitrogenBy similarity1
Metal bindingi266ZincBy similarity1
Metal bindingi282ZincBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei518GlutamateCombined sources3 Publications1
<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>Sitei614Functional determinant of NMDA receptorsBy 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q12879

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-438066, Unblocking of NMDA receptors, glutamate binding and activation
R-HSA-6794361, Neurexins and neuroligins
R-HSA-8849932, Synaptic adhesion-like molecules
R-HSA-9022699, MECP2 regulates neuronal receptors and channels
R-HSA-9609736, Assembly and cell surface presentation of NMDA receptors
R-HSA-9617324, Negative regulation of NMDA receptor-mediated neuronal transmission
R-HSA-9620244, Long-term potentiation

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

More...SignaLinki		Q12879

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q12879

Protein family/group databases

Transport Classification Database

More...TCDBi		1.A.10.1.20, the glutamate-gated ion channel (gic) family of neurotransmitter receptors

<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%5Fand%5Ftaxonomy%5Fsection">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 2A
Short name:
GluN2A
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-1
N-methyl D-aspartate receptor subtype 2A
Short name:
NMDAR2A1 Publication
Short name:
NR2A
Short name:
hNR2A1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:GRIN2A
Synonyms:NMDAR2A
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 16

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:4585, GRIN2A

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		138253, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q12879

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000183454.14

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 domaini23 – 555ExtracellularBy similarityAdd BLAST533
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei556 – 576HelicalBy similarityAdd BLAST21
Topological domaini577 – 600CytoplasmicBy similarityAdd BLAST24
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Intramembranei601 – 620Discontinuously helicalBy similarityAdd BLAST20
Topological domaini621 – 625CytoplasmicBy similarity5
Transmembranei626 – 645HelicalBy similarityAdd BLAST20
Topological domaini646 – 816ExtracellularBy similarityAdd BLAST171
Transmembranei817 – 837HelicalBy similarityAdd BLAST21
Topological domaini838 – 1464CytoplasmicBy similarityAdd BLAST627

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, 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

Epilepsy, focal, with speech disorder and with or without mental retardation (FESD)12 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA highly variable neurologic disorder with features ranging from severe early-onset seizures associated with delayed psychomotor development, persistent speech difficulties, and mental retardation 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, mental retardation and speech dyspraxia, and benign epilepsy with centrotemporal spikes.
Related information in OMIM
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_07034579P → R in FESD. 1 PublicationCorresponds to variant dbSNP:rs1250662891EnsemblClinVar.1
Natural variantiVAR_070346184I → S in FESD; unknown pathological significance. 1 Publication1
Natural variantiVAR_070347231C → Y in FESD; unknown pathological significance. 1 Publication1
Natural variantiVAR_070348243A → V in FESD; results in reduced high-affinity zinc mediated inhibition. 1 Publication1
Natural variantiVAR_070349290A → V in FESD. 1 PublicationCorresponds to variant dbSNP:rs199528312EnsemblClinVar.1
Natural variantiVAR_070350295G → S in FESD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs568484876EnsemblClinVar.1
Natural variantiVAR_070351370R → W in FESD. 1 PublicationCorresponds to variant dbSNP:rs761168789Ensembl.1
Natural variantiVAR_070352436C → R in FESD; decreased protein abundance; loss of localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency and decreased glycine potency. 2 PublicationsCorresponds to variant dbSNP:rs1555496111EnsemblClinVar.1
Natural variantiVAR_070353483G → R in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency. 2 Publications1
Natural variantiVAR_070354504R → W in FESD; decreased protein abundance; decreased localization to the cell membrane; no significant effect on calcium ion transmembrane import into cytosol. 2 PublicationsCorresponds to variant dbSNP:rs1360906241EnsemblClinVar.1
Natural variantiVAR_079933506V → A in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency. 1 PublicationCorresponds to variant dbSNP:rs796052543EnsemblClinVar.1
Natural variantiVAR_070355518R → H in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by affected receptor kinetics. 2 PublicationsCorresponds to variant dbSNP:rs397518470EnsemblClinVar.1
Natural variantiVAR_070356531T → M in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by affected receptor kinetics. 2 PublicationsCorresponds to variant dbSNP:rs397518468EnsemblClinVar.1
Natural variantiVAR_070357547Missing in FESD. 1 Publication1
Natural variantiVAR_070358548A → T in FESD; no effect on localization to the cell membrane; loss of glutamate-gated calcium ion channel activity. 2 Publications1
Natural variantiVAR_069382552P → R in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency with delay in rise time and slower deactivation time course. 2 PublicationsCorresponds to variant dbSNP:rs397518450EnsemblClinVar.1
Natural variantiVAR_065899615N → K in FESD; the mutant receptor has decreased calcium permeability; shows a dominant-negative effect. 1 PublicationCorresponds to variant dbSNP:rs397518447EnsemblClinVar.1
Natural variantiVAR_069383649L → V in FESD. 1 PublicationCorresponds to variant dbSNP:rs397514557EnsemblClinVar.1
Natural variantiVAR_070359652F → V in FESD; affects receptor kinetics. 1 PublicationCorresponds to variant dbSNP:rs397518471EnsemblClinVar.1
Natural variantiVAR_070360669K → N in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency. 2 Publications1
Natural variantiVAR_079935685V → G in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency. 1 PublicationCorresponds to variant dbSNP:rs796052548EnsemblClinVar.1
Natural variantiVAR_070361694I → T in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and decreased open probability. 2 Publications1
Natural variantiVAR_070362699P → S in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency and decreased open probability. 2 PublicationsCorresponds to variant dbSNP:rs1555491648EnsemblClinVar.1
Natural variantiVAR_070363705M → V in FESD; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and decreased open probability. 2 Publications1
Natural variantiVAR_070364714E → K in FESD; decreased protein abundance; no effect on localization to the cell membrane; no significant effect on calcium ion transmembrane import into cytosol. 2 Publications1
Natural variantiVAR_078110716A → D in FESD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1057519552EnsemblClinVar.1
Natural variantiVAR_070365716A → T in FESD; 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:rs762659685Ensembl.1
Natural variantiVAR_070366727A → T in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and decreased open probability. 2 PublicationsCorresponds to variant dbSNP:rs1555488144EnsemblClinVar.1
Natural variantiVAR_070367731D → N in FESD; decreased protein abundance; decreased localization to the cell membrane; decreased glutamate-gated calcium ion channel activity characterized by drastically decreased glutamate agonist potency, decreased glycine agonist potency, reduced amplitude of current response, shortened synaptic-like response time course, decreased channel open probability and enhanced sensitivity to negative allosteric modulators. 3 PublicationsCorresponds to variant dbSNP:rs796052549EnsemblClinVar.1
Natural variantiVAR_070368734V → L in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency. 2 Publications1
Natural variantiVAR_070369772K → E in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and decreased open probability. 2 Publications1
Natural variantiVAR_072750812L → M in FESD; increase in receptor response to agonists; decrease in the actions of endogenous negative modulators; increase in channel open probability; prolonged deactivation time course. 1 Publication1
Natural variantiVAR_070370814I → T in FESD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs780654733EnsemblClinVar.1
Natural variantiVAR_071626817M → V in FESD; gain-of-function characterized by enhanced agonist potency, reduced sensitivity to endogenous negative inhibitors, prolonged synaptic-like response time course, increased single-channel mean open time and increased channel open probability. 2 PublicationsCorresponds to variant dbSNP:rs796052551EnsemblClinVar.1
Natural variantiVAR_070371904I → F in FESD. 1 PublicationCorresponds to variant dbSNP:rs1555482933EnsemblClinVar.1
Natural variantiVAR_070372933D → N in FESD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs933322445Ensembl.1
Natural variantiVAR_070373976N → S in FESD. 1 PublicationCorresponds to variant dbSNP:rs886039239EnsemblClinVar.1
Natural variantiVAR_0703741251D → N in FESD. 1 Publication1
A chromosomal aberration involving GRIN2A has been found in a family with epilepsy and neurodevelopmental defects. Translocation t(16;17)(p13.2;q11.2).
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.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi552P → A: Changed glutamate-gated calcium ion channel activity characterized by increased desensitization. 1 Publication1
Mutagenesisi552P → G: Changed glutamate-gated calcium ion channel activity characterized by accelerated response activation time and increased desensitization. 1 Publication1
Mutagenesisi552P → I: Changed glutamate-gated calcium ion channel activity characterized by increased desensitization. 1 Publication1
Mutagenesisi552P → 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. 1 Publication1
Mutagenesisi552P → L: No effect on localization to the cell membrane. Changed glutamate-gated calcium ion channel activity characterized by increased desensitization. 1 Publication1
Mutagenesisi552P → 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. 1 Publication1

Keywords - Diseasei

Disease variant, Epilepsy

Organism-specific databases

DisGeNET

More...DisGeNETi		2903

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

More...GeneReviewsi		GRIN2A

MalaCards human disease database

More...MalaCardsi		GRIN2A
MIMi245570, phenotype

Open Targets

More...OpenTargetsi		ENSG00000183454

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

More...Orphaneti		725, Continuous spikes and waves during sleep
289266, Early-onset epileptic encephalopathy and intellectual disability due to GRIN2A mutation
98818, Landau-Kleffner syndrome
1945, Rolandic epilepsy
163721, Rolandic epilepsy-speech dyspraxia syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28979

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q12879, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1972

Drug and drug target database

More...DrugBanki		DB00659, Acamprosate
DB06151, Acetylcysteine
DB01238, Aripiprazole
DB00289, Atomoxetine
DB00843, Donepezil
DB00228, Enflurane
DB11823, Esketamine
DB00949, Felbamate
DB13146, Fluciclovine (18F)
DB06741, Gavestinel
DB00142, Glutamic acid
DB00145, Glycine
DB00874, Guaifenesin
DB01159, Halothane
DB06738, Ketobemidone
DB09409, Magnesium acetate tetrahydrate
DB09481, Magnesium carbonate
DB01043, Memantine
DB00454, Meperidine
DB00333, Methadone
DB04896, Milnacipran
DB00312, Pentobarbital
DB01174, Phenobarbital
DB01708, Prasterone
DB00418, Secobarbital
DB01520, Tenocyclidine
DB00193, Tramadol

DrugCentral

More...DrugCentrali		Q12879

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		456

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		GRIN2A

Domain mapping of disease mutations (DMDM)

More...DMDMi		14285603

<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 – 22Sequence analysisAdd BLAST22
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001157323 – 1464Glutamate receptor ionotropic, NMDA 2AAdd BLAST1442

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi75N-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 bondi87 ↔ 320By similarity
Glycosylationi340N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi380N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi429 ↔ 455Combined sources3 Publications
Disulfide bondi436 ↔ 456Combined sources3 Publications
Glycosylationi443N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi444N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi541N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi687N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi745 ↔ 800By 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 residuei890PhosphoserineBy similarity1
Modified residuei929PhosphoserineBy similarity1
Modified residuei1025PhosphoserineBy similarity1
Modified residuei1059PhosphoserineBy similarity1
Modified residuei1062PhosphoserineBy similarity1
Modified residuei1198PhosphoserineBy similarity1
Modified residuei1291PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q12879

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

More...PaxDbi		Q12879

PeptideAtlas

More...PeptideAtlasi		Q12879

PRoteomics IDEntifications database

More...PRIDEi		Q12879

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		58998 [Q12879-1]
61175

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q12879, 6 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q12879

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

More...PhosphoSitePlusi		Q12879

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000183454, Expressed in primary visual cortex and 157 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q12879, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q12879, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000183454, Tissue enriched (brain)

<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%5Fsection">'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%5Fsection">'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:28105280). Can also form heterotetrameric channels that contain at least one zeta subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B. In vivo, the subunit composition may depend on the expression levels of the different subunits.

Found in a complex with GRIN1, GRIN3A and PPP2CB (By similarity).

Found in a complex with GRIN1 and GRIN3B (By similarity).

Interacts with AIP1 (By similarity).

Interacts with HIP1 and NETO1.

Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes (By similarity).

Interacts with PDZ domains of PATJ and DLG4.

Interacts with LRFN2 (By similarity).

Interacts with RPH3A and DLG4; this ternary complex regulates NMDA receptor composition at postsynaptic membranes (By similarity).

Interacts with SORCS2 (By similarity).

Interacts with ARC; preventing ARC oligomerization (By similarity).

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		109160, 57 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2202, NMDA receptor complex, GluN1-GluN2A
CPX-294, NMDA receptor complex, GluN1-GluN2A-GluN2B

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q12879

Database of interacting proteins

More...DIPi		DIP-40798N

Protein interaction database and analysis system

More...IntActi		Q12879, 6 interactors

Molecular INTeraction database

More...MINTi		Q12879

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000379818

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q12879

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q12879, protein

<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

11464
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		Q12879

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q12879

<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>Regioni511 – 513Glutamate bindingCombined sources3 Publications3
Regioni599 – 620Pore-formingBy similarityAdd BLAST22
Regioni689 – 690Glutamate bindingBy similarity2
Regioni730 – 731Glutamate bindingBy similarity2

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>Motifi1462 – 1464PDZ-bindingCurated3

<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

Contains an N-terminal domain, a ligand-binding domain and a transmembrane domain. Agonist binding to the extracellular ligand-binding domains triggers channel gating.By similarity
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

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR2A/GRIN2A subfamily. [View classification]Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1053, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156222

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_002598_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q12879

Identification of Orthologs from Complete Genome Data

More...OMAi		PKYPRDC

Database of Orthologous Groups

More...OrthoDBi		188544at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q12879

TreeFam database of animal gene trees

More...TreeFami		TF314731

Family and domain databases

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00664

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q12879-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGRVGYWTLL VLPALLVWRG PAPSAAAEKG PPALNIAVML GHSHDVTERE 
        60         70         80         90        100
LRTLWGPEQA AGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF 
       110        120        130        140        150
GDDTDQEAVA QMLDFISSHT FVPILGIHGG ASMIMADKDP TSTFFQFGAS 
       160        170        180        190        200
IQQQATVMLK IMQDYDWHVF SLVTTIFPGY REFISFVKTT VDNSFVGWDM 
       210        220        230        240        250
QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL SEARSLGLTG 
       260        270        280        290        300
YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGIGILT 
       310        320        330        340        350
TAASSMLEKF SYIPEAKASC YGQMERPEVP MHTLHPFMVN VTWDGKDLSF 
       360        370        380        390        400
TEEGYQVHPR LVVIVLNKDR EWEKVGKWEN HTLSLRHAVW PRYKSFSDCE 
       410        420        430        440        450
PDDNHLSIVT LEEAPFVIVE DIDPLTETCV RNTVPCRKFV KINNSTNEGM 
       460        470        480        490        500
NVKKCCKGFC IDILKKLSRT VKFTYDLYLV TNGKHGKKVN NVWNGMIGEV 
       510        520        530        540        550
VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS NGTVSPSAFL 
       560        570        580        590        600
EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT 
       610        620        630        640        650
IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA 
       660        670        680        690        700
AFMIQEEFVD QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY 
       710        720        730        740        750
MHQYMTKFNQ KGVEDALVSL KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI 
       760        770        780        790        800
GSGYIFATTG YGIALQKGSP WKRQIDLALL QFVGDGEMEE LETLWLTGIC 
       810        820        830        840        850
HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL FYWKLRFCFT 
       860        870        880        890        900
GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS 
       910        920        930        940        950
AKNISSMSNM NSSRMDSPKR AADFIQRGSL IMDMVSDKGN LMYSDNRSFQ 
       960        970        980        990       1000
GKESIFGDNM NELQTFVANR QKDNLNNYVF QGQHPLTLNE SNPNTVEVAV 
      1010       1020       1030       1040       1050
STESKANSRP RQLWKKSVDS IRQDSLSQNP VSQRDEATAE NRTHSLKSPR 
      1060       1070       1080       1090       1100
YLPEEMAHSD ISETSNRATC HREPDNSKNH KTKDNFKRSV ASKYPKDCSE 
      1110       1120       1130       1140       1150
VERTYLKTKS SSPRDKIYTI DGEKEPGFHL DPPQFVENVT LPENVDFPDP 
      1160       1170       1180       1190       1200
YQDPSENFRK GDSTLPMNRN PLHNEEGLSN NDQYKLYSKH FTLKDKGSPH 
      1210       1220       1230       1240       1250
SETSERYRQN STHCRSCLSN MPTYSGHFTM RSPFKCDACL RMGNLYDIDE 
      1260       1270       1280       1290       1300
DQMLQETGNP ATGEQVYQQD WAQNNALQLQ KNKLRISRQH SYDNIVDKPR 
      1310       1320       1330       1340       1350
ELDLSRPSRS ISLKDRERLL EGNFYGSLFS VPSSKLSGKK SSLFPQGLED 
      1360       1370       1380       1390       1400
SKRSKSLLPD HTSDNPFLHS HRDDQRLVIG RCPSDPYKHS LPSQAVNDSY 
      1410       1420       1430       1440       1450
LRSSLRSTAS YCSRDSRGHN DVYISEHVMP YAANKNNMYS TPRVLNSCSN 
      1460 
RRVYKKMPSI ESDV
Length:1,464
Mass (Da):165,283
Last modified:November 1, 1996 - v1
<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:iAF5EDD599EC0B1E3
GO
Isoform 2 (identifier: Q12879-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1464: NPATGEQVYQ...KKMPSIESDV → MTNAWLLGDAPRTLTNTRCHPRR

Show »
Length:1,281
Mass (Da):144,431
Checksum:i7454CF24F5BE8373
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 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5GZ52F5GZ52_HUMAN
Glutamate receptor
GRIN2A
1,124Annotation score:

Annotation score:2 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>
A0A6Q8PGD2A0A6Q8PGD2_HUMAN
Glutamate receptor
GRIN2A
1,307Annotation score:

Annotation score:2 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>
A0A6Q8PHM7A0A6Q8PHM7_HUMAN
Glutamate receptor
GRIN2A
796Annotation score:

Annotation score:2 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>
A0A1B0GUT1A0A1B0GUT1_HUMAN
Glutamate receptor ionotropic, NMDA...
GRIN2A
200Annotation 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>
A0A1B0GU35A0A1B0GU35_HUMAN
Glutamate receptor ionotropic, NMDA...
GRIN2A
10Annotation 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>
A0A1B0GVW1A0A1B0GVW1_HUMAN
Glutamate receptor ionotropic, NMDA...
GRIN2A
19Annotation 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06772557P → L Found in a cutaneous malignant melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_07034579P → R in FESD. 1 PublicationCorresponds to variant dbSNP:rs1250662891EnsemblClinVar.1
Natural variantiVAR_079929143T → I Found in a patient with autism spectrum disorder; unknown pathological significance. 1 Publication1
Natural variantiVAR_067726183F → I Found in a cutaneous malignant melanoma sample; somatic mutation; also found in a patient with benign epilepsy with centrotemporal spike. 2 PublicationsCorresponds to variant dbSNP:rs587780353EnsemblClinVar.1
Natural variantiVAR_070346184I → S in FESD; unknown pathological significance. 1 Publication1
Natural variantiVAR_079930189T → N Found in a patient with schizophrenia; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1377082706Ensembl.1
Natural variantiVAR_070347231C → Y in FESD; unknown pathological significance. 1 Publication1
Natural variantiVAR_070348243A → V in FESD; results in reduced high-affinity zinc mediated inhibition. 1 Publication1
Natural variantiVAR_067727252D → N Found in a cutaneous malignant melanoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs868215122Ensembl.1
Natural variantiVAR_010938270K → E1 Publication1
Natural variantiVAR_067728278S → F Found in a cutaneous malignant melanoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs148531310Ensembl.1
Natural variantiVAR_070349290A → V in FESD. 1 PublicationCorresponds to variant dbSNP:rs199528312EnsemblClinVar.1
Natural variantiVAR_070350295G → S in FESD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs568484876EnsemblClinVar.1
Natural variantiVAR_079931336P → S1 PublicationCorresponds to variant dbSNP:rs148511104EnsemblClinVar.1
Natural variantiVAR_071624349S → F Found in a cutaneous malignant melanoma sample. 1 Publication1
Natural variantiVAR_070351370R → W in FESD. 1 PublicationCorresponds to variant dbSNP:rs761168789Ensembl.1
Natural variantiVAR_067729371E → K Found in a cutaneous malignant melanoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs149344082Ensembl.1
Natural variantiVAR_067730373E → K Found in a cutaneous malignant melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_078109380N → D Found in a patient with neonatal onset epileptic encephalopathy; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1057519551EnsemblClinVar.1
Natural variantiVAR_070352436C → R in FESD; decreased protein abundance; loss of localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency and decreased glycine potency. 2 PublicationsCorresponds to variant dbSNP:rs1555496111EnsemblClinVar.1
Natural variantiVAR_067731449G → E Found in a cutaneous malignant melanoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs139033056Ensembl.1
Natural variantiVAR_079932452V → M No effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency. 2 PublicationsCorresponds to variant dbSNP:rs145956175EnsemblClinVar.1
Natural variantiVAR_067732459F → S Found in a cutaneous malignant melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_070353483G → R in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency. 2 Publications1
Natural variantiVAR_070354504R → W in FESD; decreased protein abundance; decreased localization to the cell membrane; no significant effect on calcium ion transmembrane import into cytosol. 2 PublicationsCorresponds to variant dbSNP:rs1360906241EnsemblClinVar.1
Natural variantiVAR_079933506V → A in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency. 1 PublicationCorresponds to variant dbSNP:rs796052543EnsemblClinVar.1
Natural variantiVAR_070355518R → H in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by affected receptor kinetics. 2 PublicationsCorresponds to variant dbSNP:rs397518470EnsemblClinVar.1
Natural variantiVAR_070356531T → M in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by affected receptor kinetics. 2 PublicationsCorresponds to variant dbSNP:rs397518468EnsemblClinVar.1
Natural variantiVAR_070357547Missing in FESD. 1 Publication1
Natural variantiVAR_070358548A → T in FESD; no effect on localization to the cell membrane; loss of glutamate-gated calcium ion channel activity. 2 Publications1
Natural variantiVAR_069382552P → R in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency with delay in rise time and slower deactivation time course. 2 PublicationsCorresponds to variant dbSNP:rs397518450EnsemblClinVar.1
Natural variantiVAR_079934576F → S1 Publication1
Natural variantiVAR_067733595H → R Found in a cutaneous malignant melanoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs551688681Ensembl.1
Natural variantiVAR_067734598S → F Found in a cutaneous malignant melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_065899615N → K in FESD; the mutant receptor has decreased calcium permeability; shows a dominant-negative effect. 1 PublicationCorresponds to variant dbSNP:rs397518447EnsemblClinVar.1
Natural variantiVAR_069383649L → V in FESD. 1 PublicationCorresponds to variant dbSNP:rs397514557EnsemblClinVar.1
Natural variantiVAR_070359652F → V in FESD; affects receptor kinetics. 1 PublicationCorresponds to variant dbSNP:rs397518471EnsemblClinVar.1
Natural variantiVAR_067735653M → I Found in a cutaneous malignant melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_070360669K → N in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency. 2 Publications1
Natural variantiVAR_079935685V → G in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency. 1 PublicationCorresponds to variant dbSNP:rs796052548EnsemblClinVar.1
Natural variantiVAR_070361694I → T in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and decreased open probability. 2 Publications1
Natural variantiVAR_070362699P → S in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency and decreased open probability. 2 PublicationsCorresponds to variant dbSNP:rs1555491648EnsemblClinVar.1
Natural variantiVAR_070363705M → V in FESD; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and decreased open probability. 2 Publications1
Natural variantiVAR_067736712G → E Found in a cutaneous malignant melanoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs143031592Ensembl.1
Natural variantiVAR_070364714E → K in FESD; decreased protein abundance; no effect on localization to the cell membrane; no significant effect on calcium ion transmembrane import into cytosol. 2 Publications1
Natural variantiVAR_078110716A → D in FESD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1057519552EnsemblClinVar.1
Natural variantiVAR_070365716A → T in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency. 2 Publications