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Entry version 188 (13 Nov 2019)
Sequence version 2 (15 Dec 1998)
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Protein

Glutamate receptor ionotropic, NMDA 2A

Gene

Grin2a

Organism
Rattus norvegicus (Rat)
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+. Sensitivity to glutamate and channel kinetics depend on the subunit composition; channels containing GRIN1 and GRIN2A have higher sensitivity to glutamate and faster kinetics than channels formed by GRIN1 and GRIN2B (PubMed:28384476). Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (By similarity).By similarity11 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Channel activity is inhibited by nM concentrations of Zn2+.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 nitrogenCombined sources1 Publication1
Metal bindingi128Zinc; via tele nitrogenCombined sources1 Publication1
Metal bindingi266ZincCombined sources1 Publication1
Metal bindingi282ZincCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

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-RNO-438066 Unblocking of NMDA receptors, glutamate binding and activation
R-RNO-8849932 Synaptic adhesion-like molecules
R-RNO-9609736 Assembly and cell surface presentation of NMDA receptors

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.A.10.1.6 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_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 2A
Short name:
GluN2A1 Publication
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-1
N-methyl D-aspartate receptor subtype 2A
Short name:
NMDAR2A1 Publication
Short name:
NR2A2 Publications
<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:Grin2a
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2737 Grin2a

<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 & Seán O’Donoghue; 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 domaini23 – 555ExtracellularCuratedAdd BLAST533
<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>Transmembranei556 – 576HelicalBy similarityAdd BLAST21
Topological domaini577 – 600CytoplasmicCuratedAdd BLAST24
<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>Intramembranei601 – 620Discontinuously helicalBy similarityAdd BLAST20
Topological domaini621 – 625CytoplasmicCurated5
Transmembranei626 – 645HelicalBy similarityAdd BLAST20
Topological domaini646 – 816ExtracellularCuratedAdd BLAST171
Transmembranei817 – 837HelicalBy similarityAdd BLAST21
Topological domaini838 – 1464CytoplasmicCuratedAdd 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

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>Mutagenesisi233K → A or R: Nearly abolishes inhibition by Zn(2+). 1 Publication1
Mutagenesisi264N → W: Nearly abolishes inhibition by Zn(2+). 1 Publication1
Mutagenesisi282D → A or H: Nearly abolishes inhibition by Zn(2+). 1 Publication1
Mutagenesisi416F → A: Decreased sensitivity to glutamate. 1 Publication1
Mutagenesisi730Y → F, L or M: Strongly decreased sensitivity to glutamate. 1 Publication1
Mutagenesisi734V → A: Decreased sensitivity to glutamate. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL310

DrugCentral

More...
DrugCentrali
Q00959

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001157623 – 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_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>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 ↔ 320Combined sources1 Publication
Glycosylationi340N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi429 ↔ 455Combined sources6 Publications
Disulfide bondi436 ↔ 456Combined sources6 Publications
Glycosylationi443N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi444N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi541N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi745 ↔ 800Combined sources4 Publications
<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 residuei882PhosphoserineCombined sources1
Modified residuei890PhosphoserineCombined sources1
Modified residuei929PhosphoserineCombined sources1
Modified residuei1025PhosphoserineCombined sources1
Modified residuei1059PhosphoserineCombined sources1
Modified residuei1062PhosphoserineCombined sources1
Modified residuei1198PhosphoserineCombined sources1
Modified residuei1291PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
Q00959

PRoteomics IDEntifications database

More...
PRIDEi
Q00959

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q00959

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

More...
PhosphoSitePlusi
Q00959

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q00959

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
Q00959

<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

Detected in brain cortex, olfactory bulb, hippocampus including the dentate gyrus, striatum, thalamus, superior colliculus, inferior colliculus, midbrain and cerebellum (at protein level) (PubMed:22960932, PubMed:9509416). Detected in brain cortex, hypothalamus and cerebellum (PubMed:1350383).3 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed during postnatal days P3 to P60, with increased expression after postnatal day 3.1 Publication

<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:1350383, PubMed:8428958, PubMed:28384476, PubMed:16281028, PubMed:23625947, PubMed:24462099, PubMed:27618671, PubMed:27916457, PubMed:28468946, PubMed:28760974, Ref. 27). Can also form heterotetrameric channels that contain at least one zeta subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B (PubMed:11160393, PubMed:11588171, PubMed:12391275, PubMed:11929923). In vivo, the subunit composition may depend on the expression levels of the different subunits (Probable).

Found in a complex with GRIN1, GRIN3A and PPP2CB (PubMed:11588171).

Found in a complex with GRIN1 and GRIN3B (PubMed:14602821).

Interacts with AIP1 (PubMed:9694864).

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 (PubMed:7569905, PubMed:9647694).

Interacts with LRFN2 (PubMed:16495444).

Interacts with RPH3A and DLG4; this ternary complex regulates NMDA receptor composition at postsynaptic membranes (PubMed:26679993).

Interacts with SORCS2 (By similarity).

Interacts with ARC; preventing ARC oligomerization (PubMed:31080121).

By similarityCurated22 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
246574, 8 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-283 NMDA receptor complex, GluN1-GluN2A
CPX-295 NMDA receptor complex, GluN1-GluN2A-GluN2B

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q00959

Database of interacting proteins

More...
DIPi
DIP-34031N

Protein interaction database and analysis system

More...
IntActi
Q00959, 7 interactors

Molecular INTeraction database

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MINTi
Q00959

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000042235

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q00959

<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

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SMRi
Q00959

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q00959

<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 sources1 Publication3
Regioni599 – 620Pore-formingBy similarityAdd BLAST22
Regioni689 – 690Glutamate bindingCombined sources2 Publications2
Regioni730 – 731Glutamate bindingCombined sources2 Publications2

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.1 Publication
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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000113802

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q00959

KEGG Orthology (KO)

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KOi
K05209

Database of Orthologous Groups

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OrthoDBi
188544at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q00959

Family and domain databases

Integrated resource of protein families, domains and functional sites

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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>. 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>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 1 potential isoform that is computationally mapped.Show allAlign All

Q00959-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGRLGYWTLL VLPALLVWRD PAQNAAAEKG PPALNIAVLL GHSHDVTERE
60 70 80 90 100
LRNLWGPEQA TGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF
110 120 130 140 150
GDDTDQEAVA QMLDFISSQT FIPILGIHGG ASMIMADKDP TSTFFQFGAS
160 170 180 190 200
IQQQATVMLK IMQDYDWHVF SLVTTIFPGY RDFISFIKTT VDNSFVGWDM
210 220 230 240 250
QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL SEARSLGLTG
260 270 280 290 300
YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGLGILT
310 320 330 340 350
TAASSMLEKF SYIPEAKASC YGQAEKPETP LHTLHQFMVN VTWDGKDLSF
360 370 380 390 400
TEEGYQVHPR LVVIVLNKDR EWEKVGKWEN QTLSLRHAVW 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
MHQYMTRFNQ RGVEDALVSL KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI
760 770 780 790 800
GSGYIFASTG 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
AKNISNMSNM NSSRMDSPKR ATDFIQRGSL IVDMVSDKGN LIYSDNRSFQ
960 970 980 990 1000
GKDSIFGDNM NELQTFVANR HKDNLSNYVF QGQHPLTLNE SNPNTVEVAV
1010 1020 1030 1040 1050
STESKGNSRP RQLWKKSMES LRQDSLNQNP VSQRDEKTAE NRTHSLKSPR
1060 1070 1080 1090 1100
YLPEEVAHSD ISETSSRATC HREPDNNKNH KTKDNFKRSM ASKYPKDCSD
1110 1120 1130 1140 1150
VDRTYMKTKA SSPRDKIYTI DGEKEPSFHL DPPQFVENIT LPENVGFPDT
1160 1170 1180 1190 1200
YQDHNENFRK GDSTLPMNRN PLHNEDGLPN NDQYKLYAKH FTLKDKGSPH
1210 1220 1230 1240 1250
SEGSDRYRQN STHCRSCLSN LPTYSGHFTM RSPFKCDACL RMGNLYDIDE
1260 1270 1280 1290 1300
DQMLQETGNP ATREEVYQQD WSQNNALQFQ KNKLRINRQH SYDNILDKPR
1310 1320 1330 1340 1350
EIDLSRPSRS ISLKDRERLL EGNLYGSLFS VPSSKLLGNK SSLFPQGLED
1360 1370 1380 1390 1400
SKRSKSLLPD HASDNPFLHT YGDDQRLVIG RCPSDPYKHS LPSQAVNDSY
1410 1420 1430 1440 1450
LRSSLRSTAS YCSRDSRGHS DVYISEHVMP YAANKNTMYS TPRVLNSCSN
1460
RRVYKKMPSI ESDV
Length:1,464
Mass (Da):165,469
Last modified:December 15, 1998 - v2
<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:iDC1528E1898DECA4
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V9C5G3V9C5_RAT
Glutamate receptor ionotropic, NMDA...
Grin2a
1,307Annotation score:

Annotation score:4 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 conflicti246L → F in BAA02498 (PubMed:8428958).Curated1
Sequence conflicti758S → T in BAA02498 (PubMed:8428958).Curated1
Sequence conflicti758S → T in AAB58801 (Ref. 4) Curated1
Sequence conflicti990E → D in AAB58801 (Ref. 4) Curated1

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
M91561 mRNA Translation: AAC03565.1
D13211 mRNA Translation: BAA02498.1
AF001423 mRNA Translation: AAB58801.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A43274

NCBI Reference Sequences

More...
RefSeqi
NP_036705.3, NM_012573.3

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24409

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24409

UCSC genome browser

More...
UCSCi
RGD:2737 rat

<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
M91561 mRNA Translation: AAC03565.1
D13211 mRNA Translation: BAA02498.1
AF001423 mRNA Translation: AAB58801.1
PIRiA43274
RefSeqiNP_036705.3, NM_012573.3

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
2A5SX-ray1.70A401-539[»]
2A5TX-ray2.00B401-539[»]
4JWXX-ray1.50A404-539[»]
A661-802[»]
4NF4X-ray2.00B402-539[»]
B661-802[»]
4NF5X-ray1.90B402-539[»]
B661-802[»]
4NF6X-ray2.10B402-539[»]
B661-802[»]
4NF8X-ray1.86B402-539[»]
B661-802[»]
5DEXX-ray2.40B402-539[»]
B661-802[»]
5I56X-ray2.28B402-539[»]
B661-800[»]
5I57X-ray1.70B402-539[»]
B661-800[»]
5I58X-ray2.52B402-539[»]
B661-800[»]
5I59X-ray2.25B402-539[»]
B661-800[»]
5JTYX-ray2.72B402-539[»]
B661-800[»]
5TPWX-ray2.91B34-393[»]
5TQ0X-ray2.70B34-393[»]
5TQ2X-ray3.29B34-393[»]
5U8CX-ray1.60B402-539[»]
A661-802[»]
5VIHX-ray2.40B402-539[»]
B566-800[»]
5VIIX-ray1.95B402-539[»]
B566-800[»]
5VIJX-ray2.10B402-539[»]
B566-800[»]
6MM9electron microscopy5.97B/D1-837[»]
6MMAelectron microscopy6.31B/D1-837[»]
6MMBelectron microscopy12.70B/D1-837[»]
6MMGelectron microscopy6.23B/D1-837[»]
6MMHelectron microscopy8.21B/D1-837[»]
6MMIelectron microscopy8.93B/D1-837[»]
6MMJelectron microscopy16.50B/D1-837[»]
6MMKelectron microscopy6.08B/D1-837[»]
6MMLelectron microscopy7.14B/D1-837[»]
6MMMelectron microscopy6.84B/D1-837[»]
6MMNelectron microscopy7.51B/D1-837[»]
6MMPelectron microscopy6.88B/D1-837[»]
6MMRelectron microscopy5.13B/D1-837[»]
6MMSelectron microscopy5.38B/D1-837[»]
6MMTelectron microscopy7.46B/D1-837[»]
6MMUelectron microscopy5.30B/D1-837[»]
6MMVelectron microscopy4.71B/D1-800[»]
6MMWelectron microscopy6.20B/D1-837[»]
6MMXelectron microscopy6.99B/D1-837[»]
SMRiQ00959
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi246574, 8 interactors
ComplexPortaliCPX-283 NMDA receptor complex, GluN1-GluN2A
CPX-295 NMDA receptor complex, GluN1-GluN2A-GluN2B
CORUMiQ00959
DIPiDIP-34031N
IntActiQ00959, 7 interactors
MINTiQ00959
STRINGi10116.ENSRNOP00000042235

Chemistry databases

BindingDBiQ00959
ChEMBLiCHEMBL310
DrugCentraliQ00959

Protein family/group databases

TCDBi1.A.10.1.6 the glutamate-gated ion channel (gic) family of neurotransmitter receptors

PTM databases

iPTMnetiQ00959
PhosphoSitePlusiQ00959
SwissPalmiQ00959
UniCarbKBiQ00959

Proteomic databases

PaxDbiQ00959
PRIDEiQ00959

Genome annotation databases

GeneIDi24409
KEGGirno:24409
UCSCiRGD:2737 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2903
RGDi2737 Grin2a

Phylogenomic databases

eggNOGiKOG1053 Eukaryota
ENOG410XNUR LUCA
HOGENOMiHOG000113802
InParanoidiQ00959
KOiK05209
OrthoDBi188544at2759
PhylomeDBiQ00959

Enzyme and pathway databases

ReactomeiR-RNO-438066 Unblocking of NMDA receptors, glutamate binding and activation
R-RNO-8849932 Synaptic adhesion-like molecules
R-RNO-9609736 Assembly and cell surface presentation of NMDA receptors

Miscellaneous databases

EvolutionaryTraceiQ00959

Protein Ontology

More...
PROi
PR:Q00959

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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiNMDE1_RAT
<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: Q00959
Secondary accession number(s): O08948, Q63728
<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 1, 1994
Last sequence update: December 15, 1998
Last modified: November 13, 2019
This is version 188 of the entry and version 2 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

<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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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