Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q01097

- NMDE2_MOUSE

UniProt

Q01097 - NMDE2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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

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
Complete GO annotation...

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

MaxQBiQ01097.
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 33-837.
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

        10         20         30         40         50
MKPSAECCSP KFWLVLAVLA VSGSKARSQK SAPSIGIAVI LVGTSDEVAI
60 70 80 90 100
KDAHEKDDFH HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVLA
110 120 130 140 150
DDTDQEAIAQ ILDFISAQTL TPILGIHGGS SMIMADKDES SMFFQFGPSI
160 170 180 190 200
EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ DFVNKIRSTI ENSFVGWELE
210 220 230 240 250
EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI FEVANSVGLT
260 270 280 290 300
GYGYTWIVPS LVAGDTDTVP SEFPTGLISV SYDEWDYGLP ARVRDGIAII
310 320 330 340 350
TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS
360 370 380 390 400
FSEDGYQMHP KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE
410 420 430 440 450
QEDDHLSIVT LEEAPFVIVE SVDPLSGTCM RNTVPCQKRI ISENKTDEEP
460 470 480 490 500
GYIKKCCKGF CIDILKKISK SVKFTYDLYL VTNGKHGKKI NGTWNGMIGE
510 520 530 540 550
VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR SNGTVSPSAF
560 570 580 590 600
LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF
610 620 630 640 650
TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL
660 670 680 690 700
AAFMIQEEYV DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA
710 720 730 740 750
EMHAYMGKFN QRGVDDALLS LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT
760 770 780 790 800
IGSGKVFAST GYGIAIQKDS GWKRQVDLAI LQLFGDGEME ELEALWLTGI
810 820 830 840 850
CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH LFYWQFRHCF
860 870 880 890 900
MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR
910 920 930 940 950
LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN
960 970 980 990 1000
NPPCEENLFS DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSTSSI
1010 1020 1030 1040 1050
DGLYDCDNPP FTTQPRSISK KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS
1060 1070 1080 1090 1100
GHDDLIRSDV SDISTHTVTY GNIEGNAAKR RKQQYKDSLK KRPASAKSRR
1110 1120 1130 1140 1150
EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK ENSPHWEHVD
1160 1170 1180 1190 1200
LTDIYKERSD DFKRDSVSGG GPCTNRSHLK HGTGDKHGVV GGVPAPWEKN
1210 1220 1230 1240 1250
LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN
1260 1270 1280 1290 1300
LYDISEDNSL QELDQPAAPV AVSSNASTTK YPQSPTNSKA QKKNRNKLRR
1310 1320 1330 1340 1350
QHSYDTFVDL QKEEAALAPR SVSLKDKGRF MDGSPYAHMF EMPAGESSFA
1360 1370 1380 1390 1400
NKSSVTTAGH HHNNPGSGYM LSKSLYPDRV TQNPFIPTFG DDQCLLHGSK
1410 1420 1430 1440 1450
SYFFRQPTVA GASKTRPDFR ALVTNKPVVS ALHGAVPGRF QKDICIGNQS
1460 1470 1480
NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV
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 33-837.
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

MaxQBi Q01097.
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

« Hide 'large scale' publications
  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 29, 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

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