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UniProtKB - Q01098 (NMDE3_MOUSE)

Entry version 186 (29 Sep 2021)
Sequence version 2 (01 Feb 1996)
Previous versions | rss
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Protein

Glutamate receptor ionotropic, NMDA 2C

Gene

Grin2c

Organism
Mus musculus (Mouse)
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:1377365).

Sensitivity to glutamate and channel kinetics depend on the subunit composition (PubMed:1377365).

Plays a role in regulating the balance between excitatory and inhibitory activity of pyramidal neurons in the prefrontal cortex (PubMed:27922130).

Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (PubMed:8987814).

3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei511GlutamateBy similarity1
Binding sitei516GlutamateBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei612Functional determinant of NMDA receptorsBy similarity1
Binding sitei729GlutamateBy 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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-438066, Unblocking of NMDA receptors, glutamate binding and activation
R-MMU-8849932, Synaptic adhesion-like molecules
R-MMU-9609736, Assembly and cell surface presentation of NMDA 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 2C
Short name:
GluN2C
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-31 Publication
N-methyl D-aspartate receptor subtype 2C
Short name:
NMDAR2C
Short name:
NR2C1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Grin2c
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:95822, Grin2c

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000020734

<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_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 domaini20 – 554ExtracellularBy similarityAdd BLAST535
<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>Transmembranei555 – 573HelicalBy similarityAdd BLAST19
Topological domaini574 – 600CytoplasmicBy similarityAdd BLAST27
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei601 – 620Discontinuously helicalBy similarityAdd BLAST20
Topological domaini621 – 627CytoplasmicBy similarity7
Transmembranei628 – 643HelicalBy similarityAdd BLAST16
Topological domaini644 – 814ExtracellularBy similarityAdd BLAST171
Transmembranei815 – 834HelicalBy similarityAdd BLAST20
Topological domaini835 – 1239CytoplasmicBy similarityAdd BLAST405

Keywords - Cellular componenti

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

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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant mice appear grossly normal (PubMed:8987814). Mossy fiber granule cells from mutant mice present a decrease of the slow component of the excitatory postsynaptic current (PubMed:8987814). Pyramidal neurons in the prefrontal cortex display a reduced dendritic spine density (PubMed:27922130). Besides, the prefrontal cortex has an altered pattern of excitatory and inhibitory synapses (PubMed:27922130). Pyramidal neurons in the prefrontal cortex display a reduced frequency of miniature excitatory postsynaptic currents (mEPSC), together with an increased frequency of miniature inhibitory postsynaptic currents (mIPSC), indicative of a shift in the balance between excitatory and inhibitory membrane currents (PubMed:27922130). The slow component of the excitatory postsynaptic current is nearly abolished in mossy fiber cells from mice lacking both Grin2a and Grin2c (PubMed:8987814). Mice lacking both Grin2a and Grin2c display subtle motor deficits; they have no visible phenotype when performing simple tasks, but have decreased ability to walk across a narrow wooden bar, and are unable to stay on a rapidly rotating rod (PubMed:8987814).2 Publications

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3832634

<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 – 19Sequence analysisAdd BLAST19
<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_000001158120 – 1239Glutamate receptor ionotropic, NMDA 2CAdd BLAST1220

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>Glycosylationi70N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi73N-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 bondi82 ↔ 317By similarity
Glycosylationi337N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi426 ↔ 453By similarity
Disulfide bondi433 ↔ 454By similarity
Glycosylationi438N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi539N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi685N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi743 ↔ 798By 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 residuei875PhosphoserineCombined sources1
Modified residuei881PhosphoserineCombined sources1
Modified residuei912PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

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

More...PaxDbi		Q01098

PRoteomics IDEntifications database

More...PRIDEi		Q01098

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		293865

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		2352, 1 N-Linked glycan (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q01098, 6 sites, 1 N-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q01098

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

More...PhosphoSitePlusi		Q01098

<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 cerebellum (at protein level) (PubMed:8987814). Detected in the granule cell layer of the cerebellum (PubMed:1377365).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000020734, Expressed in cerebellar cortex and 127 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q01098, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q01098, MM

<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:1377365). Can also form heterotetrameric channels that contain at least one zeta subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B (By similarity). In vivo, the subunit composition may depend on the expression levels of the different subunits (Probable).

Interacts with PDZ domains of PATJ and DLG4 (By similarity).

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

By similarityCurated1 Publication

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		200070, 6 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-292, NMDA receptor complex, GluN1-GluN2C

Protein interaction database and analysis system

More...IntActi		Q01098, 1 interactor

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000102164

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q01098, 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

3D structure databases

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

More...SMRi		Q01098

Database of comparative protein structure models

More...ModBasei		Search...

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni509 – 511Glutamate bindingBy similarity3
Regioni601 – 620Pore-formingBy similarityAdd BLAST20
Regioni687 – 688Glutamate bindingBy similarity2
Regioni918 – 988DisorderedSequence analysisAdd BLAST71

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>Motifi1237 – 1239PDZ-binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi918 – 936Polar residuesSequence analysisAdd BLAST19
Compositional biasi937 – 952Pro residuesSequence analysisAdd BLAST16

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

A hydrophobic region that gives rise to the prediction of a transmembrane span does not cross the membrane, but is part of a discontinuously helical region that dips into the membrane and is probably part of the pore and of the selectivity filter.By similarity

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

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR2C/GRIN2C 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		ENSGT00940000156964

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_002039_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q01098

Identification of Orthologs from Complete Genome Data

More...OMAi		YPYKQKL

Database of Orthologous Groups

More...OrthoDBi		188544at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q01098

TreeFam database of animal gene trees

More...TreeFami		TF314731

Family and domain databases

Integrated resource of protein families, domains and functional sites

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

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00177, NMDARECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53822, SSF53822, 1 hit

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

<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.

Q01098-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGGALGPALL LTSLLGAWAG LGAGQGEQAV TVAVVFGSSG PLQAQARTRL 
        60         70         80         90        100
TPQNFLDLPL EIQPLTIGVN NTNPSSILTQ ICGLLGAARV HGIVFEDNVD 
       110        120        130        140        150
TEAVAQLLDF VSSQTHVPIL SISGGSAVVL TPKEPGSAFL QLGVSLEQQL 
       160        170        180        190        200
QVLFKVLEEY DWSAFAVITS LHPGHALFLE GVRAVADASY LSWRLLDVLT 
       210        220        230        240        250
LELGPGGPRA RTQRLLRQVD APVLVAYCSR EEAEVLFAEA AQAGLVGPGH 
       260        270        280        290        300
VWLVPNLALG STDAPPAAFP VGLISVVTES WRLSLRQKVR DGVAILALGA 
       310        320        330        340        350
HSYRRQYGTL PAPAGDCRSH PGPVSPAREA FYRHLLNVTW EGRDFSFSPG 
       360        370        380        390        400
GYLVQPTMVV IALNRHRLWE MVGRWDHGVL YMKYPVWPRY STSLQPVVDS 
       410        420        430        440        450
RHLTVATLEE RPFVIVESPD PGTGGCVPNT VPCRRQSNHT FSSGDITPYT 
       460        470        480        490        500
KLCCKGFCID ILKKLAKVVK FSYDLYLVTN GKHGKRVRGV WNGMIGEVYY 
       510        520        530        540        550
KRADMAIGSL TINEERSEII DFSVPFVETG ISVMVARSNG TVSPSAFLEP 
       560        570        580        590        600
YSPAVWVMMF VMCLTVVAIT VFMFEYFSPV SYNQNLTKGK KSGGPSFTIG 
       610        620        630        640        650
KSVWLLWALV FNNSVPIENP RGTTSKIMVL VWAFFAVIFL ASYTANLAAF 
       660        670        680        690        700
MIQEQYIDTV SGLSDKKFQR PQDQYPPFRF GTVPNGSTER NIRSNYRDMH 
       710        720        730        740        750
THMVKFNQRS VEDALTSLKM GKLDAFIYDA AVLNYMAGKD EGCKLVTIGS 
       760        770        780        790        800
GKVFATTGYG IAMQKDSHWK RAIDLALLQF LGDGETQKLE TVWLSGICHN 
       810        820        830        840        850
EKNEVMSSKL DIDNMAGVFY MLLVAMGLAL LVFAWEHLVY WKLRHSVPSS 
       860        870        880        890        900
SQLDFLLAFS RGIYSCFNGV QSLPSPARPP SPDLTAGSAQ ANVLKMLQAA 
       910        920        930        940        950
RDMVSTADVS GSLDRATRTI ENWGNNRRAP APTTSGPRSC TPGPPGQPSP 
       960        970        980        990       1000
SGWRPPGGGR TPLARRAPQP PARPATCAGS PQPDVSRASC RHAWDARWPV 
      1010       1020       1030       1040       1050
RVGHQGSHLS ASERRALPER SLLHAHCHYS SFPRAERSGR PFLPLFPEPP 
      1060       1070       1080       1090       1100
EPDDLPLLGP EQLARREALL RAAWARGPRP RHASLPSSVA EAFTRSNPLP 
      1110       1120       1130       1140       1150
ARCTGHACAC PCPQSRPSCR HVAQTQSLRL PSYREACVEG VPAGVAATWQ 
      1160       1170       1180       1190       1200
PRQHVCLHTH THLPFCWGTV CRHPPPCSSH SPWLIGTWEP PSHRGRTLGL 
      1210       1220       1230 
GTGYRDSGVL EEVSREACGT QGFPRSCTWR RISSLESEV
Length:1,239
Mass (Da):135,420
Last modified:February 1, 1996 - 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:i793E8E731E20C3C9
GO

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
D10694 mRNA Translation: BAA01536.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS25624.1

Protein sequence database of the Protein Information Resource

More...PIRi		I49705

NCBI Reference Sequences

More...RefSeqi		NP_034480.2, NM_010350.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000003351; ENSMUSP00000003351; ENSMUSG00000020734
ENSMUST00000106554; ENSMUSP00000102164; ENSMUSG00000020734

Database of genes from NCBI RefSeq genomes

More...GeneIDi		14813

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:14813

UCSC genome browser

More...UCSCi		uc007mgx.1, mouse

<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
D10694 mRNA Translation: BAA01536.1
CCDSiCCDS25624.1
PIRiI49705
RefSeqiNP_034480.2, NM_010350.2

3D structure databases

SMRiQ01098
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi200070, 6 interactors
ComplexPortaliCPX-292, NMDA receptor complex, GluN1-GluN2C
IntActiQ01098, 1 interactor
STRINGi10090.ENSMUSP00000102164

Chemistry databases

ChEMBLiCHEMBL3832634

PTM databases

GlyConnecti2352, 1 N-Linked glycan (1 site)
GlyGeniQ01098, 6 sites, 1 N-linked glycan (1 site)
iPTMnetiQ01098
PhosphoSitePlusiQ01098

Proteomic databases

PaxDbiQ01098
PRIDEiQ01098
ProteomicsDBi293865

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		Q01098, 3 sequenced antibodies

Antibodypedia a portal for validated antibodies

More...Antibodypediai		19474, 285 antibodies

The DNASU plasmid repository

More...DNASUi		14813

Genome annotation databases

EnsembliENSMUST00000003351; ENSMUSP00000003351; ENSMUSG00000020734
ENSMUST00000106554; ENSMUSP00000102164; ENSMUSG00000020734
GeneIDi14813
KEGGimmu:14813
UCSCiuc007mgx.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2905
MGIiMGI:95822, Grin2c
VEuPathDBiHostDB:ENSMUSG00000020734

Phylogenomic databases

eggNOGiKOG1053, Eukaryota
GeneTreeiENSGT00940000156964
HOGENOMiCLU_002039_1_0_1
InParanoidiQ01098
OMAiYPYKQKL
OrthoDBi188544at2759
PhylomeDBiQ01098
TreeFamiTF314731

Enzyme and pathway databases

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

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		14813, 3 hits in 64 CRISPR screens

Protein Ontology

More...PROi		PR:Q01098
RNActiQ01098, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000020734, Expressed in cerebellar cortex and 127 other tissues
ExpressionAtlasiQ01098, baseline and differential
GenevisibleiQ01098, MM

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

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 nameiNMDE3_MOUSE
<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: Q01098
<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: February 1, 1996
Last modified: September 29, 2021
This is version 186 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

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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