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Entry version 173 (03 Jul 2019)
Sequence version 2 (01 Feb 1996)
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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

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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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

<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 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.<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
<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
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

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PRIDEi
Q01098

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2352

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.

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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 101 organ(s), highest expression level in cerebellum lobe

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q01098 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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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

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

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IntActi
Q01098, 1 interactor

Molecular INTeraction database

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MINTi
Q01098

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000102164

<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

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SMRi
Q01098

Database of comparative protein structure models

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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

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

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

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

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1053 Eukaryota
ENOG410XNUR LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156964

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231061

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q01098

KEGG Orthology (KO)

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KOi
K05211

Identification of Orthologs from Complete Genome Data

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OMAi
PSYREAC

Database of Orthologous Groups

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OrthoDBi
188544at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q01098

TreeFam database of animal gene trees

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TreeFami
TF314731

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

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PRINTSi
PR00177 NMDARECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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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

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
D10694 mRNA Translation: BAA01536.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS25624.1

Protein sequence database of the Protein Information Resource

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PIRi
I49705

NCBI Reference Sequences

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RefSeqi
NP_034480.2, NM_010350.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000003351; ENSMUSP00000003351; ENSMUSG00000020734
ENSMUST00000106554; ENSMUSP00000102164; ENSMUSG00000020734

Database of genes from NCBI RefSeq genomes

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GeneIDi
14813

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:14813

UCSC genome browser

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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
MINTiQ01098
STRINGi10090.ENSMUSP00000102164

Chemistry databases

ChEMBLiCHEMBL3832634

PTM databases

GlyConnecti2352
iPTMnetiQ01098
PhosphoSitePlusiQ01098

Proteomic databases

PaxDbiQ01098
PRIDEiQ01098

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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

Phylogenomic databases

eggNOGiKOG1053 Eukaryota
ENOG410XNUR LUCA
GeneTreeiENSGT00940000156964
HOGENOMiHOG000231061
InParanoidiQ01098
KOiK05211
OMAiPSYREAC
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

Protein Ontology

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PROi
PR:Q01098

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000020734 Expressed in 101 organ(s), highest expression level in cerebellum lobe
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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: July 3, 2019
This is version 173 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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