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Q01097

- NMDE2_MOUSE

UniProt

Q01097 - NMDE2_MOUSE

Protein

Glutamate receptor ionotropic, NMDA 2B

Gene

Grin2b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (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.1 Publication

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

    GO - Biological processi

    1. behavioral fear response Source: MGI
    2. behavioral response to pain Source: MGI
    3. calcium ion transmembrane transport Source: GOC
    4. calcium ion transport Source: MGI
    5. cation transport Source: MGI
    6. detection of mechanical stimulus involved in sensory perception of pain Source: MGI
    7. fear response Source: MGI
    8. in utero embryonic development Source: MGI
    9. ionotropic glutamate receptor signaling pathway Source: GOC
    10. ion transmembrane transport Source: GOC
    11. learning Source: MGI
    12. learning or memory Source: UniProtKB
    13. memory Source: MGI
    14. regulation of excitatory postsynaptic membrane potential Source: MGI
    15. regulation of neuronal synaptic plasticity Source: UniProtKB
    16. regulation of postsynaptic membrane potential Source: MGI
    17. regulation of synaptic plasticity Source: MGI
    18. response to ethanol Source: MGI
    19. sensory organ development Source: MGI
    20. startle response Source: MGI
    21. suckling behavior Source: MGI
    22. synaptic transmission Source: MGI
    23. 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

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:95821. Grin2b.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell surface Source: BHF-UCL
    3. membrane Source: MGI
    4. neuronal postsynaptic density Source: BHF-UCL
    5. neuron projection Source: BHF-UCL
    6. N-methyl-D-aspartate selective glutamate receptor complex Source: MGI
    7. postsynaptic density Source: MGI
    8. postsynaptic membrane Source: MGI
    9. presynaptic membrane Source: UniProtKB
    10. synapse Source: MGI
    11. synaptic vesicle Source: MGI

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 14821456Glutamate receptor ionotropic, NMDA 2BPRO_0000011578Add
    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 – 9621Phosphotyrosine1 Publication
    Modified residuei1039 – 10391Phosphotyrosine1 Publication
    Modified residuei1109 – 11091Phosphotyrosine1 Publication
    Modified residuei1133 – 11331Phosphotyrosine1 Publication
    Modified residuei1155 – 11551Phosphotyrosine1 Publication
    Modified residuei1303 – 13031Phosphoserine; by DAPK11 Publication
    Modified residuei1472 – 14721Phosphotyrosine1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity.3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ01097.
    PRIDEiQ01097.

    PTM databases

    PhosphoSiteiQ01097.

    Expressioni

    Gene expression databases

    GenevestigatoriQ01097.

    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, DLG4 and MAGI3 By similarity. Interacts with HIP1 and NETO1. Interacts with DAPK1.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Actn2Q9JI914EBI-400125,EBI-299169
    Ap2a1P174262EBI-400125,EBI-775189
    Camk2aP117986EBI-400125,EBI-400384
    Dapk1Q80YE78EBI-400125,EBI-2584874
    Dlg4Q6210816EBI-400125,EBI-300895

    Protein-protein interaction databases

    BioGridi200069. 71 interactions.
    DIPiDIP-31568N.
    IntActiQ01097. 187 interactions.
    MINTiMINT-135847.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01097.
    SMRiQ01097. Positions 33-836.
    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 – 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 DAPK1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1480 – 14823PDZ-bindingBy similarity

    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.
    InParanoidiQ01097.
    KOiK05210.
    PhylomeDBiQ01097.

    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.

    Q01097-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPSAECCSP KFWLVLAVLA VSGSKARSQK SAPSIGIAVI LVGTSDEVAI     50
    KDAHEKDDFH HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVLA 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 HGTGDKHGVV GGVPAPWEKN 1200
    LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN 1250
    LYDISEDNSL QELDQPAAPV AVSSNASTTK YPQSPTNSKA QKKNRNKLRR 1300
    QHSYDTFVDL QKEEAALAPR SVSLKDKGRF MDGSPYAHMF EMPAGESSFA 1350
    NKSSVTTAGH HHNNPGSGYM LSKSLYPDRV TQNPFIPTFG DDQCLLHGSK 1400
    SYFFRQPTVA GASKTRPDFR ALVTNKPVVS ALHGAVPGRF QKDICIGNQS 1450
    NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV 1482
    Length:1,482
    Mass (Da):165,959
    Last modified:June 20, 2001 - v3
    Checksum:iB8C3FA10E9A4B36D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti99 – 991L → F in BAB22483. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10651 mRNA. Translation: BAA01498.2.
    AK002963 mRNA. Translation: BAB22483.1.
    CCDSiCCDS20648.1.
    PIRiI49704.
    RefSeqiNP_032197.3. NM_008171.3.
    UniGeneiMm.436649.

    Genome annotation databases

    GeneIDi14812.
    KEGGimmu:14812.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10651 mRNA. Translation: BAA01498.2 .
    AK002963 mRNA. Translation: BAB22483.1 .
    CCDSi CCDS20648.1.
    PIRi I49704.
    RefSeqi NP_032197.3. NM_008171.3.
    UniGenei Mm.436649.

    3D structure databases

    ProteinModelPortali Q01097.
    SMRi Q01097. Positions 33-836.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200069. 71 interactions.
    DIPi DIP-31568N.
    IntActi Q01097. 187 interactions.
    MINTi MINT-135847.

    Chemistry

    BindingDBi Q01097.
    ChEMBLi CHEMBL3442.
    GuidetoPHARMACOLOGYi 457.

    PTM databases

    PhosphoSitei Q01097.

    Proteomic databases

    PaxDbi Q01097.
    PRIDEi Q01097.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 14812.
    KEGGi mmu:14812.

    Organism-specific databases

    CTDi 2904.
    MGIi MGI:95821. Grin2b.

    Phylogenomic databases

    eggNOGi NOG282132.
    HOGENOMi HOG000113802.
    HOVERGENi HBG052635.
    InParanoidi Q01097.
    KOi K05210.
    PhylomeDBi Q01097.

    Miscellaneous databases

    NextBioi 287003.
    PROi Q01097.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori Q01097.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: SEQUENCE REVISION.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-337.
      Strain: C57BL/6J.
      Tissue: Brain.
    4. "Regulation of NMDA receptor function by Fyn-mediated tyrosine phosphorylation."
      Nakazawa T., Tezuka T., Yamamoto T.
      Nihon Shinkei Seishin Yakurigaku Zasshi 22:165-167(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-1472.
    5. "Cloning and characterization of a novel NMDA receptor subunit NR3B: a dominant subunit that reduces calcium permeability."
      Matsuda K., Kamiya Y., Matsuda S., Yuzaki M.
      Brain Res. Mol. Brain Res. 100:43-52(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
    6. "Specific assembly with the NMDA receptor 3B subunit controls surface expression and calcium permeability of NMDA receptors."
      Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.
      J. Neurosci. 23:10064-10073(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
    7. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    8. "NMDA receptor function and NMDA receptor-dependent phosphorylation of huntingtin is altered by the endocytic protein HIP1."
      Metzler M., Gan L., Wong T.P., Liu L., Helm J., Liu L., Georgiou J., Wang Y., Bissada N., Cheng K., Roder J.C., Wang Y.T., Hayden M.R.
      J. Neurosci. 27:2298-2308(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIP1.
    9. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
      Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
      Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain cortex.
    10. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-962; TYR-1039; TYR-1109; TYR-1133 AND TYR-1155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    11. "Neto1 is a novel CUB-domain NMDA receptor-interacting protein required for synaptic plasticity and learning."
      Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M., Clapcote S.J., Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M., Roder J.C., Salter M.W., McInnes R.R.
      PLoS Biol. 7:E41-E41(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NETO1.
    12. "DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage in stroke."
      Tu W., Xu X., Peng L., Zhong X., Zhang W., Soundarapandian M.M., Balel C., Wang M., Jia N., Zhang W., Lew F., Chan S.L., Chen Y., Lu Y.
      Cell 140:222-234(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-1303, INTERACTION WITH DAPK1.

    Entry informationi

    Entry nameiNMDE2_MOUSE
    AccessioniPrimary (citable) accession number: Q01097
    Secondary accession number(s): Q9DCB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 20, 2001
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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

    External Data

    Dasty 3