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Q00960

- NMDE2_RAT

UniProt

Q00960 - NMDE2_RAT

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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

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 heterodimerization activity Source: RGD
  12. receptor binding Source: RGD
  13. 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 amine Source: RGD
  25. response to amphetamine Source: RGD
  26. response to calcium ion Source: RGD
  27. response to carbohydrate Source: RGD
  28. response to cocaine Source: RGD
  29. response to cytokine Source: RGD
  30. response to electrical stimulus Source: RGD
  31. response to ethanol Source: RGD
  32. response to fungicide Source: RGD
  33. response to growth hormone Source: RGD
  34. response to magnesium ion Source: RGD
  35. response to manganese ion Source: RGD
  36. response to mechanical stimulus Source: RGD
  37. response to methylmercury Source: RGD
  38. response to organic cyclic compound Source: RGD
  39. response to other organism Source: RGD
  40. response to toxic substance Source: RGD
  41. rhythmic process Source: RGD
  42. 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

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 557531ExtracellularSequence AnalysisAdd
BLAST
Transmembranei558 – 57821HelicalSequence AnalysisAdd
BLAST
Topological domaini579 – 63456CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei635 – 65521HelicalSequence AnalysisAdd
BLAST
Topological domaini656 – 817162ExtracellularSequence AnalysisAdd
BLAST
Transmembranei818 – 83821HelicalSequence AnalysisAdd
BLAST
Topological domaini839 – 1482644CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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
Camk2aP112752EBI-396905,EBI-2640645
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 – 4411Combined sources
Helixi47 – 504Combined sources
Helixi53 – 553Combined sources
Beta strandi64 – 7310Combined sources
Helixi78 – 9114Combined sources
Beta strandi94 – 10310Combined sources
Helixi107 – 11913Combined sources
Beta strandi123 – 1275Combined sources
Helixi128 – 1314Combined sources
Beta strandi143 – 1475Combined sources
Helixi150 – 16314Combined sources
Beta strandi168 – 1758Combined sources
Helixi179 – 19113Combined sources
Beta strandi198 – 2058Combined sources
Beta strandi211 – 2133Combined sources
Helixi215 – 2206Combined sources
Beta strandi226 – 2327Combined sources
Helixi234 – 24512Combined sources
Turni246 – 2483Combined sources
Beta strandi250 – 2534Combined sources
Beta strandi255 – 2584Combined sources
Helixi260 – 2634Combined sources
Beta strandi275 – 2817Combined sources
Turni284 – 2863Combined sources
Helixi289 – 30820Combined sources
Turni309 – 3113Combined sources
Turni322 – 3265Combined sources
Helixi327 – 3304Combined sources
Helixi336 – 3394Combined sources
Beta strandi355 – 3595Combined sources
Beta strandi362 – 3676Combined sources
Beta strandi369 – 3713Combined sources
Beta strandi373 – 3797Combined sources
Beta strandi384 – 3874Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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

« Hide

        10         20         30         40         50
MKPSAECCSP KFWLVLAVLA VSGSKARSQK SPPSIGIAVI LVGTSDEVAI
60 70 80 90 100
KDAHEKDDFH HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVFA
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 HGTGEKHGVV GGVPAPWEKN
1210 1220 1230 1240 1250
LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN
1260 1270 1280 1290 1300
LYDISEDNSL QELDQPAAPV AVTSNASSTK YPQSPTNSKA QKKNRNKLRR
1310 1320 1330 1340 1350
QHSYDTFVDL QKEEAALAPR SVSLKDKGRF MDGSPYAHMF EMPAGESSFA
1360 1370 1380 1390 1400
NKSSVPTAGH HHNNPGSGYM LSKSLYPDRV TQNPFIPTFG DDQCLLHGSK
1410 1420 1430 1440 1450
SYFFRQPTVA GASKTRPDFR ALVTNKPVVV TLHGAVPGRF QKDICIGNQS
1460 1470 1480
NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 145 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