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Q13224

- NMDE2_HUMAN

UniProt

Q13224 - NMDE2_HUMAN

Protein

Glutamate receptor ionotropic, NMDA 2B

Gene

GRIN2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (20 Jun 2001)
      Previous versions | rss
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    Functioni

    NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi127 – 1271ZincBy similarity
    Metal bindingi284 – 2841ZincBy similarity
    Sitei615 – 6151Functional determinant of NMDA receptorsBy similarity

    GO - Molecular functioni

    1. calcium channel activity Source: Ensembl
    2. extracellular-glutamate-gated ion channel activity Source: RefGenome
    3. glycine binding Source: UniProtKB
    4. N-methyl-D-aspartate selective glutamate receptor activity Source: RefGenome
    5. protein binding Source: UniProtKB
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. behavioral fear response Source: Ensembl
    2. behavioral response to pain Source: Ensembl
    3. detection of mechanical stimulus involved in sensory perception of pain Source: Ensembl
    4. glutamate receptor signaling pathway Source: ProtInc
    5. in utero embryonic development Source: Ensembl
    6. ionotropic glutamate receptor signaling pathway Source: RefGenome
    7. ion transmembrane transport Source: RefGenome
    8. learning Source: Ensembl
    9. learning or memory Source: ProtInc
    10. memory Source: Ensembl
    11. regulation of excitatory postsynaptic membrane potential Source: Ensembl
    12. regulation of synaptic plasticity Source: Ensembl
    13. response to ethanol Source: UniProtKB
    14. sensory organ development Source: Ensembl
    15. startle response Source: Ensembl
    16. suckling behavior Source: Ensembl
    17. synaptic transmission Source: Reactome
    18. synaptic transmission, glutamatergic Source: RefGenome
    19. transport Source: ProtInc

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
    REACT_20642. CREB phosphorylation through the activation of CaMKII.
    SignaLinkiQ13224.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate receptor ionotropic, NMDA 2B
    Short name:
    GluN2B
    Alternative name(s):
    Glutamate [NMDA] receptor subunit epsilon-2
    N-methyl D-aspartate receptor subtype 2B
    Short name:
    NMDAR2B
    Short name:
    NR2B
    N-methyl-D-aspartate receptor subunit 3
    Short name:
    NR3
    Short name:
    hNR3
    Gene namesi
    Name:GRIN2B
    Synonyms:NMDAR2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:4586. GRIN2B.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell surface Source: BHF-UCL
    3. dendrite Source: RefGenome
    4. integral component of plasma membrane Source: ProtInc
    5. neuron projection Source: BHF-UCL
    6. N-methyl-D-aspartate selective glutamate receptor complex Source: UniProtKB
    7. plasma membrane Source: Reactome
    8. postsynaptic density Source: Ensembl
    9. postsynaptic membrane Source: RefGenome
    10. synaptic vesicle Source: Ensembl

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, autosomal dominant 6 (MRD6) [MIM:613970]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti553 – 5531P → L in MRD6. 1 Publication
    VAR_069384
    Natural varianti682 – 6821R → C in MRD6; analysis of agonist dose-response curves reveal no differences in the affinities of wild-type and mutant receptors for glutamate and glycine. 1 Publication
    VAR_065900
    A chromosomal aberrations involving GRIN2B has been found in patients with mental retardation. Translocations t(9;12)(p23;p13.1) and t(10;12)(q21.1;p13.1) with a common breakpoint in 12p13.1.

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi613970. phenotype.
    Orphaneti178469. Autosomal dominant nonsyndromic intellectual disability.
    3451. West syndrome.
    PharmGKBiPA28980.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 14841458Glutamate receptor ionotropic, NMDA 2BPRO_0000011577Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi86 ↔ 321By similarity
    Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi348 – 3481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi444 – 4441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi542 – 5421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi688 – 6881N-linked (GlcNAc...)Sequence Analysis
    Modified residuei962 – 9621PhosphotyrosineBy similarity
    Modified residuei1039 – 10391PhosphotyrosineBy similarity
    Modified residuei1109 – 11091PhosphotyrosineBy similarity
    Modified residuei1133 – 11331PhosphotyrosineBy similarity
    Modified residuei1155 – 11551PhosphotyrosineBy similarity
    Modified residuei1303 – 13031Phosphoserine; by DAPK1By similarity
    Modified residuei1474 – 14741PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ13224.
    PeptideAtlasiQ13224.
    PRIDEiQ13224.

    PTM databases

    PhosphoSiteiQ13224.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ13224.
    BgeeiQ13224.
    CleanExiHS_GRIN2B.
    GenevestigatoriQ13224.

    Interactioni

    Subunit structurei

    Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A or GRIN3B). Found in a complex with GRIN1 and GRIN3B. Found in a complex with GRIN1, GRIN3A and PPP2CB. Interacts with PDZ domains of INADL and DLG4. Interacts with HIP1 and NETO1 By similarity. Interacts with MAGI3. Interacts with DAPK1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAMK2AQ9UQM73EBI-2256942,EBI-1383687
    Dlg3Q629364EBI-2256942,EBI-349596From a different organism.
    DLG4P783522EBI-2256942,EBI-80389
    Dlg4P310162EBI-2256942,EBI-375655From a different organism.
    PPP1CAP621392EBI-2256942,EBI-2008988From a different organism.

    Protein-protein interaction databases

    BioGridi109161. 25 interactions.
    DIPiDIP-41002N.
    IntActiQ13224. 13 interactions.
    MINTiMINT-127466.
    STRINGi9606.ENSP00000279593.

    Structurei

    Secondary structure

    1
    1484
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni423 – 4264
    Beta strandi429 – 4313
    Beta strandi440 – 4423
    Helixi448 – 4536
    Helixi461 – 47212
    Helixi496 – 5027
    Beta strandi507 – 5093
    Helixi517 – 5204
    Beta strandi529 – 5357
    Helixi666 – 6705
    Helixi673 – 6753
    Turni678 – 6803
    Helixi690 – 6989
    Helixi700 – 7067
    Helixi714 – 72310
    Beta strandi724 – 7274
    Helixi733 – 7408
    Turni743 – 7453
    Beta strandi757 – 7626
    Helixi773 – 78513
    Helixi789 – 7979

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S11model-A403-543[»]
    B660-801[»]
    1S2Smodel-A405-543[»]
    B660-801[»]
    2IPVmodel-X404-768[»]
    ProteinModelPortaliQ13224.
    SMRiQ13224. Positions 32-836.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 557531ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini579 – 63456CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini656 – 817162ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini839 – 1484646CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei558 – 57821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei635 – 65521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei818 – 83821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1292 – 130413Interaction with DAPK1By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1482 – 14843PDZ-bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi984 – 9896Poly-His
    Compositional biasi1361 – 13644Poly-His

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG282132.
    HOGENOMiHOG000113802.
    HOVERGENiHBG052635.
    InParanoidiQ13224.
    KOiK05210.
    OMAiCTNRSHL.
    OrthoDBiEOG72ZCD1.
    PhylomeDBiQ13224.
    TreeFamiTF314731.

    Family and domain databases

    InterProiIPR001828. ANF_lig-bd_rcpt.
    IPR019594. Glu_rcpt_Glu/Gly-bd.
    IPR001320. Iontro_glu_rcpt.
    IPR001508. NMDA_rcpt.
    IPR018884. NMDAR2_C.
    IPR028082. Peripla_BP_I.
    IPR001638. SBP_bac_3.
    [Graphical view]
    PfamiPF01094. ANF_receptor. 1 hit.
    PF00060. Lig_chan. 1 hit.
    PF10565. NMDAR2_C. 1 hit.
    PF00497. SBP_bac_3. 1 hit.
    [Graphical view]
    PRINTSiPR00177. NMDARECEPTOR.
    SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
    SM00079. PBPe. 1 hit.
    [Graphical view]
    SUPFAMiSSF53822. SSF53822. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q13224-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPRAECCSP KFWLVLAVLA VSGSRARSQK SPPSIGIAVI LVGTSDEVAI     50
    KDAHEKDDFH HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVFA 100
    DDTDQEAIAQ ILDFISAQTL TPILGIHGGS SMIMADKDES SMFFQFGPSI 150
    EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ DFVNKIRSTI ENSFVGWELE 200
    EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI FEVANSVGLT 250
    GYGYTWIVPS LVAGDTDTVP AEFPTGLISV SYDEWDYGLP ARVRDGIAII 300
    TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS 350
    FSEDGYQMHP KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE 400
    QEDDHLSIVT LEEAPFVIVE SVDPLSGTCM RNTVPCQKRI VTENKTDEEP 450
    GYIKKCCKGF CIDILKKISK SVKFTYDLYL VTNGKHGKKI NGTWNGMIGE 500
    VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR SNGTVSPSAF 550
    LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF 600
    TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL 650
    AAFMIQEEYV DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA 700
    EMHAYMGKFN QRGVDDALLS LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT 750
    IGSGKVFAST GYGIAIQKDS GWKRQVDLAI LQLFGDGEME ELEALWLTGI 800
    CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH LFYWQFRHCF 850
    MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR 900
    LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN 950
    NPPCEENLFS DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSASSI 1000
    DGLYDCDNPP FTTQSRSISK KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS 1050
    GHDDLIRSDV SDISTHTVTY GNIEGNAAKR RKQQYKDSLK KRPASAKSRR 1100
    EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK ENSPHWEHVD 1150
    LTDIYKERSD DFKRDSVSGG GPCTNRSHIK HGTGDKHGVV SGVPAPWEKN 1200
    LTNVEWEDRS GGNFCRSCPS KLHNYSTTVT GQNSGRQACI RCEACKKAGN 1250
    LYDISEDNSL QELDQPAAPV AVTSNASTTK YPQSPTNSKA QKKNRNKLRR 1300
    QHSYDTFVDL QKEEAALAPR SVSLKDKGRF MDGSPYAHMF EMSAGESTFA 1350
    NNKSSVPTAG HHHHNNPGGG YMLSKSLYPD RVTQNPFIPT FGDDQCLLHG 1400
    SKSYFFRQPT VAGASKARPD FRALVTNKPV VSALHGAVPA RFQKDICIGN 1450
    QSNPCVPNNK NPRAFNGSSN GHVYEKLSSI ESDV 1484
    Length:1,484
    Mass (Da):166,367
    Last modified:June 20, 2001 - v3
    Checksum:i40AEB12BE6E50CEF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti434 – 4341V → A in AAD00659. 1 PublicationCurated
    Sequence conflicti745 – 7451G → A in AAA69920. (PubMed:7959773)Curated
    Sequence conflicti773 – 7731K → N in AAA69920. (PubMed:7959773)Curated
    Sequence conflicti773 – 7731K → N in AAA74930. (PubMed:7959773)Curated
    Sequence conflicti796 – 7961W → C in AAA69920. (PubMed:7959773)Curated
    Sequence conflicti796 – 7961W → C in AAA74930. (PubMed:7959773)Curated
    Sequence conflicti888 – 8881T → P in AAA69920. (PubMed:7959773)Curated
    Sequence conflicti888 – 8881T → P in AAA74930. (PubMed:7959773)Curated
    Sequence conflicti902 – 9021L → V in AAA69920. (PubMed:7959773)Curated
    Sequence conflicti902 – 9021L → V in AAA74930. (PubMed:7959773)Curated
    Sequence conflicti920 – 9212SA → RP in AAB60368. (PubMed:7999784)Curated
    Sequence conflicti958 – 9581L → S in AAA69920. (PubMed:7959773)Curated
    Sequence conflicti958 – 9581L → S in AAA74930. (PubMed:7959773)Curated
    Sequence conflicti980 – 9823VYQ → DHY in AAA69920. (PubMed:7959773)Curated
    Sequence conflicti1056 – 10561I → M in AAA69920. (PubMed:7959773)Curated
    Sequence conflicti1167 – 11671V → I in AAB49993. (PubMed:8768735)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti407 – 4071S → N.1 Publication
    VAR_011317
    Natural varianti553 – 5531P → L in MRD6. 1 Publication
    VAR_069384
    Natural varianti682 – 6821R → C in MRD6; analysis of agonist dose-response curves reveal no differences in the affinities of wild-type and mutant receptors for glutamate and glycine. 1 Publication
    VAR_065900

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U90278 mRNA. Translation: AAB49993.1.
    U88963 mRNA. Translation: AAD00659.1.
    U11287 mRNA. Translation: AAB60368.1.
    BC113618 mRNA. Translation: AAI13619.1.
    BC113620 mRNA. Translation: AAI13621.1.
    U28758 mRNA. Translation: AAA74930.1.
    U28861 mRNA. Translation: AAA69919.1.
    U28862 mRNA. Translation: AAA69920.1.
    CCDSiCCDS8662.1.
    PIRiI39066.
    S52086.
    RefSeqiNP_000825.2. NM_000834.3.
    UniGeneiHs.654430.

    Genome annotation databases

    GeneIDi2904.
    KEGGihsa:2904.
    UCSCiuc001rbt.2. human.

    Polymorphism databases

    DMDMi14548162.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U90278 mRNA. Translation: AAB49993.1 .
    U88963 mRNA. Translation: AAD00659.1 .
    U11287 mRNA. Translation: AAB60368.1 .
    BC113618 mRNA. Translation: AAI13619.1 .
    BC113620 mRNA. Translation: AAI13621.1 .
    U28758 mRNA. Translation: AAA74930.1 .
    U28861 mRNA. Translation: AAA69919.1 .
    U28862 mRNA. Translation: AAA69920.1 .
    CCDSi CCDS8662.1.
    PIRi I39066.
    S52086.
    RefSeqi NP_000825.2. NM_000834.3.
    UniGenei Hs.654430.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S11 model - A 403-543 [» ]
    B 660-801 [» ]
    1S2S model - A 405-543 [» ]
    B 660-801 [» ]
    2IPV model - X 404-768 [» ]
    ProteinModelPortali Q13224.
    SMRi Q13224. Positions 32-836.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109161. 25 interactions.
    DIPi DIP-41002N.
    IntActi Q13224. 13 interactions.
    MINTi MINT-127466.
    STRINGi 9606.ENSP00000279593.

    Chemistry

    BindingDBi Q13224.
    ChEMBLi CHEMBL2094124.
    DrugBanki DB00949. Felbamate.
    DB00502. Haloperidol.
    DB00142. L-Glutamic Acid.
    DB00836. Loperamide.
    DB01043. Memantine.
    GuidetoPHARMACOLOGYi 457.

    PTM databases

    PhosphoSitei Q13224.

    Polymorphism databases

    DMDMi 14548162.

    Proteomic databases

    PaxDbi Q13224.
    PeptideAtlasi Q13224.
    PRIDEi Q13224.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2904.
    KEGGi hsa:2904.
    UCSCi uc001rbt.2. human.

    Organism-specific databases

    CTDi 2904.
    GeneCardsi GC12M013714.
    H-InvDB HIX0036873.
    HGNCi HGNC:4586. GRIN2B.
    MIMi 138252. gene.
    613970. phenotype.
    neXtProti NX_Q13224.
    Orphaneti 178469. Autosomal dominant nonsyndromic intellectual disability.
    3451. West syndrome.
    PharmGKBi PA28980.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282132.
    HOGENOMi HOG000113802.
    HOVERGENi HBG052635.
    InParanoidi Q13224.
    KOi K05210.
    OMAi CTNRSHL.
    OrthoDBi EOG72ZCD1.
    PhylomeDBi Q13224.
    TreeFami TF314731.

    Enzyme and pathway databases

    Reactomei REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
    REACT_20642. CREB phosphorylation through the activation of CaMKII.
    SignaLinki Q13224.

    Miscellaneous databases

    GeneWikii GRIN2B.
    GenomeRNAii 2904.
    NextBioi 11499.
    PROi Q13224.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13224.
    Bgeei Q13224.
    CleanExi HS_GRIN2B.
    Genevestigatori Q13224.

    Family and domain databases

    InterProi IPR001828. ANF_lig-bd_rcpt.
    IPR019594. Glu_rcpt_Glu/Gly-bd.
    IPR001320. Iontro_glu_rcpt.
    IPR001508. NMDA_rcpt.
    IPR018884. NMDAR2_C.
    IPR028082. Peripla_BP_I.
    IPR001638. SBP_bac_3.
    [Graphical view ]
    Pfami PF01094. ANF_receptor. 1 hit.
    PF00060. Lig_chan. 1 hit.
    PF10565. NMDAR2_C. 1 hit.
    PF00497. SBP_bac_3. 1 hit.
    [Graphical view ]
    PRINTSi PR00177. NMDARECEPTOR.
    SMARTi SM00918. Lig_chan-Glu_bd. 1 hit.
    SM00079. PBPe. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53822. SSF53822. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human N-methyl-D-aspartate receptor modulatory subunit hNR3: cloning and sequencing of the cDNA and primary structure of the protein."
      Adams S.L., Foldes R.L., Kamboj R.K.
      Biochim. Biophys. Acta 1260:105-108(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-407.
      Tissue: Fetal brain.
    2. "Cloning and functional characterization of human heteromeric N-methyl-D-aspartate receptors."
      Hess S.D., Daggett L.P., Crona J., Deal C., Lu C.-C., Urrutia A., Chavez-Noriega L., Ellis S.B., Johnson E.C., Velicelebi G.
      J. Pharmacol. Exp. Ther. 278:808-816(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    3. "Cloning of GRIN2B human subunit."
      Mandich P., Schito A.M., Pizzuti A., Ratti A.
      Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cerebellum.
    5. "Mapping of the human NMDAR2B receptor subunit gene (GRIN2B) to chromosome 12p12."
      Mandich P., Schito A.M., Bellone E., Antonacci R., Finelli P., Rocchi M., Ajmar F.
      Genomics 22:216-218(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-294 AND 661-1089.
    6. "mRNA distribution in adult human brain of GRIN2B, a N-methyl-D-aspartate (NMDA) receptor subunit."
      Schito A.M., Pizzuti A., Di Maria E., Schenone A., Ratti A., Defferrari R., Bellone E., Mancardi G.L., Ajmar F., Mandich P.
      Neurosci. Lett. 239:49-53(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase."
      Wu Y., Dowbenko D., Spencer S., Laura R., Lee J., Gu Q., Lasky L.A.
      J. Biol. Chem. 275:21477-21485(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAGI3.
    8. Cited for: CHROMOSOMAL TRANSLOCATIONS, VARIANT MRD6 CYS-682.
    9. Cited for: VARIANT MRD6 LEU-553.

    Entry informationi

    Entry nameiNMDE2_HUMAN
    AccessioniPrimary (citable) accession number: Q13224
    Secondary accession number(s): Q12919
    , Q13220, Q13225, Q14CU4, Q9UM56
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: June 20, 2001
    Last modified: October 1, 2014
    This is version 150 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3