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Q00960

- NMDE2_RAT

UniProt

Q00960 - NMDE2_RAT

Protein

Glutamate receptor ionotropic, NMDA 2B

Gene

Grin2b

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      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 – 1271Zinc
    Metal bindingi284 – 2841Zinc
    Sitei615 – 6151Functional determinant of NMDA receptorsBy similarity

    GO - Molecular functioni

    1. beta-catenin binding Source: RGD
    2. cell adhesion molecule binding Source: RGD
    3. D2 dopamine receptor binding Source: RGD
    4. drug binding Source: RGD
    5. extracellular-glutamate-gated ion channel activity Source: RGD
    6. interleukin-1 receptor binding Source: RGD
    7. ionotropic glutamate receptor activity Source: RGD
    8. ionotropic glutamate receptor binding Source: RGD
    9. neurotransmitter binding Source: RGD
    10. N-methyl-D-aspartate selective glutamate receptor activity Source: RGD
    11. protein binding Source: UniProtKB
    12. protein heterodimerization activity Source: RGD
    13. receptor binding Source: RGD
    14. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. action potential Source: RGD
    2. associative learning Source: RGD
    3. cellular response to amino acid stimulus Source: RGD
    4. cellular response to dsRNA Source: RGD
    5. cellular response to growth factor stimulus Source: RGD
    6. cellular response to lipid Source: RGD
    7. cellular response to magnesium starvation Source: RGD
    8. cellular response to manganese ion Source: RGD
    9. cellular response to organic cyclic compound Source: RGD
    10. cerebral cortex development Source: RGD
    11. hippocampus development Source: RGD
    12. ionotropic glutamate receptor signaling pathway Source: RGD
    13. ion transmembrane transport Source: GOC
    14. learning or memory Source: RGD
    15. long-term memory Source: RGD
    16. memory Source: UniProtKB
    17. multicellular organismal response to stress Source: RGD
    18. positive regulation of cell death Source: RGD
    19. positive regulation of glutamate secretion Source: UniProtKB
    20. positive regulation of synaptic transmission Source: RGD
    21. receptor clustering Source: RGD
    22. regulation of long-term neuronal synaptic plasticity Source: RGD
    23. regulation of MAPK cascade Source: UniProtKB
    24. response to acid chemical Source: RGD
    25. response to amine Source: RGD
    26. response to amphetamine Source: RGD
    27. response to calcium ion Source: RGD
    28. response to carbohydrate Source: RGD
    29. response to cocaine Source: RGD
    30. response to cytokine Source: RGD
    31. response to electrical stimulus Source: RGD
    32. response to ethanol Source: RGD
    33. response to fungicide Source: RGD
    34. response to growth hormone Source: RGD
    35. response to magnesium ion Source: RGD
    36. response to manganese ion Source: RGD
    37. response to mechanical stimulus Source: RGD
    38. response to methylmercury Source: RGD
    39. response to organic cyclic compound Source: RGD
    40. response to other organism Source: RGD
    41. rhythmic process Source: RGD
    42. synaptic transmission, glutamatergic Source: RefGenome

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding, Zinc

    Protein family/group databases

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

    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
    Gene namesi
    Name:Grin2b
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2738. Grin2b.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. dendritic spine Source: RGD
    3. neuron projection Source: UniProtKB
    4. N-methyl-D-aspartate selective glutamate receptor complex Source: UniProtKB
    5. postsynaptic density Source: RGD
    6. postsynaptic membrane Source: RefGenome
    7. presynaptic membrane Source: UniProtKB
    8. synapse Source: UniProtKB
    9. synaptic cleft Source: RGD
    10. terminal bouton Source: RGD
    11. Z disc Source: RGD

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi60 – 601H → A: Normal zinc binding. 1 Publication
    Mutagenesisi127 – 1271H → A: Reduced zinc binding.
    Mutagenesisi283 – 2831D → A: Slightly reduced zinc binding.
    Mutagenesisi284 – 2841E → A: Reduced zinc binding.
    Mutagenesisi311 – 3111H → A: Normal zinc binding. 1 Publication
    Mutagenesisi359 – 3591H → A: Normal zinc binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 14821456Glutamate receptor ionotropic, NMDA 2BPRO_0000011579Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi74 – 741N-linked (GlcNAc...)1 Publication
    Disulfide bondi86 ↔ 3211 Publication
    Glycosylationi341 – 3411N-linked (GlcNAc...)1 Publication
    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 residuei1472 – 14721PhosphotyrosineBy 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

    PaxDbiQ00960.
    PRIDEiQ00960.

    PTM databases

    PhosphoSiteiQ00960.

    Expressioni

    Gene expression databases

    GenevestigatoriQ00960.

    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, GRIN3A and PPP2CB. Found in a complex with GRIN1 and GRIN3B. Interacts with MAGI3. Interacts with HIP1 and Neto1 By similarity. Interacts with PDZ domains of INADL and DLG4. Interacts with DAPK1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Camk2aP117983EBI-396905,EBI-400384From a different organism.
    Dlg3Q629366EBI-396905,EBI-349596
    Dlg4P310168EBI-396905,EBI-375655
    InadlQ63ZW74EBI-396905,EBI-8366894From a different organism.
    Lrfn2Q460M52EBI-396905,EBI-877185

    Protein-protein interaction databases

    BioGridi246575. 11 interactions.
    DIPiDIP-33702N.
    IntActiQ00960. 16 interactions.
    MINTiMINT-104014.
    STRINGi10116.ENSRNOP00000011697.

    Structurei

    Secondary structure

    1
    1482
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 4411
    Helixi47 – 504
    Helixi53 – 553
    Beta strandi64 – 7310
    Helixi78 – 9114
    Beta strandi94 – 10310
    Helixi107 – 11913
    Beta strandi123 – 1275
    Helixi128 – 1314
    Beta strandi143 – 1475
    Helixi150 – 16314
    Beta strandi168 – 1758
    Helixi179 – 19113
    Beta strandi198 – 2058
    Beta strandi211 – 2133
    Helixi215 – 2206
    Beta strandi226 – 2327
    Helixi234 – 24512
    Turni246 – 2483
    Beta strandi250 – 2534
    Beta strandi255 – 2584
    Helixi260 – 2634
    Beta strandi275 – 2817
    Turni284 – 2863
    Helixi289 – 30820
    Turni309 – 3113
    Turni322 – 3265
    Helixi327 – 3304
    Helixi336 – 3394
    Beta strandi355 – 3595
    Beta strandi362 – 3676
    Beta strandi369 – 3713
    Beta strandi373 – 3797
    Beta strandi384 – 3874

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3JPWX-ray2.80A32-394[»]
    3JPYX-ray3.21A32-394[»]
    3QELX-ray2.60B/D31-394[»]
    3QEMX-ray3.00B/D31-394[»]
    4PE5X-ray3.96B/D27-852[»]
    ProteinModelPortaliQ00960.
    SMRiQ00960. Positions 404-802.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00960.

    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 – 1482644CytoplasmicSequence 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
    Motifi1480 – 14823PDZ-binding

    Compositional bias

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

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG282132.
    HOGENOMiHOG000113802.
    HOVERGENiHBG052635.
    InParanoidiQ00960.
    KOiK05210.
    PhylomeDBiQ00960.

    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.

    Q00960-1 [UniParc]FASTAAdd to Basket

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    MKPSAECCSP KFWLVLAVLA VSGSKARSQK 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 SEFPTGLISV SYDEWDYGLP ARVRDGIAII 300
    TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS 350
    FSEDGYQMHP KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE 400
    QEDDHLSIVT LEEAPFVIVE SVDPLSGTCM RNTVPCQKRI ISENKTDEEP 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 PHSIGSTSSI 1000
    DGLYDCDNPP FTTQPRSISK KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS 1050
    GHDDLIRSDV SDISTHTVTY GNIEGNAAKR RKQQYKDSLK KRPASAKSRR 1100
    EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK ENSPHWEHVD 1150
    LTDIYKERSD DFKRDSVSGG GPCTNRSHLK HGTGEKHGVV GGVPAPWEKN 1200
    LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN 1250
    LYDISEDNSL QELDQPAAPV AVTSNASSTK YPQSPTNSKA QKKNRNKLRR 1300
    QHSYDTFVDL QKEEAALAPR SVSLKDKGRF MDGSPYAHMF EMPAGESSFA 1350
    NKSSVPTAGH HHNNPGSGYM LSKSLYPDRV TQNPFIPTFG DDQCLLHGSK 1400
    SYFFRQPTVA GASKTRPDFR ALVTNKPVVV TLHGAVPGRF QKDICIGNQS 1450
    NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV 1482
    Length:1,482
    Mass (Da):166,071
    Last modified:June 1, 1994 - v1
    Checksum:iAEF8B9DF3C1B0D5D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1256 – 12561E → K in AAA50554. (PubMed:7524561)Curated
    Sequence conflicti1430 – 14312VT → SA in AAA50554. (PubMed:7524561)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M91562 mRNA. Translation: AAA41714.1.
    U11419 mRNA. Translation: AAA50554.1.
    PIRiB43274.
    RefSeqiNP_036706.1. NM_012574.1.
    UniGeneiRn.9711.

    Genome annotation databases

    GeneIDi24410.
    KEGGirno:24410.
    UCSCiRGD:2738. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M91562 mRNA. Translation: AAA41714.1 .
    U11419 mRNA. Translation: AAA50554.1 .
    PIRi B43274.
    RefSeqi NP_036706.1. NM_012574.1.
    UniGenei Rn.9711.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3JPW X-ray 2.80 A 32-394 [» ]
    3JPY X-ray 3.21 A 32-394 [» ]
    3QEL X-ray 2.60 B/D 31-394 [» ]
    3QEM X-ray 3.00 B/D 31-394 [» ]
    4PE5 X-ray 3.96 B/D 27-852 [» ]
    ProteinModelPortali Q00960.
    SMRi Q00960. Positions 404-802.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246575. 11 interactions.
    DIPi DIP-33702N.
    IntActi Q00960. 16 interactions.
    MINTi MINT-104014.
    STRINGi 10116.ENSRNOP00000011697.

    Chemistry

    BindingDBi Q00960.
    ChEMBLi CHEMBL2096669.
    GuidetoPHARMACOLOGYi 457.

    Protein family/group databases

    TCDBi 1.A.10.1.6. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

    PTM databases

    PhosphoSitei Q00960.

    Proteomic databases

    PaxDbi Q00960.
    PRIDEi Q00960.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24410.
    KEGGi rno:24410.
    UCSCi RGD:2738. rat.

    Organism-specific databases

    CTDi 2904.
    RGDi 2738. Grin2b.

    Phylogenomic databases

    eggNOGi NOG282132.
    HOGENOMi HOG000113802.
    HOVERGENi HBG052635.
    InParanoidi Q00960.
    KOi K05210.
    PhylomeDBi Q00960.

    Miscellaneous databases

    EvolutionaryTracei Q00960.
    NextBioi 603231.
    PROi Q00960.

    Gene expression databases

    Genevestigatori Q00960.

    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. "Heteromeric NMDA receptors: molecular and functional distinction of subtypes."
      Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H., Burnashev N., Sakmann B., Seeburg P.H.
      Science 256:1217-1221(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor."
      Sullivan J.M., Traynelis S.F., Chen H.S., Escobar W., Heinemann S.F., Lipton S.A.
      Neuron 13:929-936(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95."
      Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H.
      Science 269:1737-1740(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLG4.
    4. "CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins."
      Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.
      Mol. Cell. Neurosci. 11:161-172(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INADL.
    5. "An NMDA receptor signaling complex with protein phosphatase 2A."
      Chan S.F., Sucher N.J.
      J. Neurosci. 21:7985-7992(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN3A AND PPP2CB.
    6. "Assembly with the NR1 subunit is required for surface expression of NR3A-containing NMDA receptors."
      Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A., Trimmer J.S., Sucher N.J., Heinemann S.F.
      J. Neurosci. 21:1228-1237(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
    7. "Association of NR3A with the N-methyl-D-aspartate receptor NR1 and NR2 subunits."
      Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B., Yasuda R.P.
      Mol. Pharmacol. 62:1119-1127(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
    8. "Characterization and comparison of the NR3A subunit of the NMDA receptor in recombinant systems and primary cortical neurons."
      Sasaki Y.F., Rothe T., Premkumar L.S., Das S., Cui J., Talantova M.V., Wong H.-K., Gong X., Chan S.F., Zhang D., Nakanishi N., Sucher N.J., Lipton S.A.
      J. Neurophysiol. 87:2052-2063(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
    9. "Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit."
      Karakas E., Simorowski N., Furukawa H.
      EMBO J. 28:3910-3920(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 32-394 IN COMPLEX WITH ZINC ION, GLYCOSYLATION AT ASN-74; HIS-127; ASP-283; GLU-284 AND ASN-341, MUTAGENESIS OF HIS-60; HIS-311 AND HIS-359, DISULFIDE BOND.

    Entry informationi

    Entry nameiNMDE2_RAT
    AccessioniPrimary (citable) accession number: Q00960
    Secondary accession number(s): Q62684
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 143 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3