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Protein

Glutamate receptor ionotropic, NMDA 2A

Gene

Grin2a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Activation requires binding of agonist to both types of subunits.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi128 – 1281ZincBy similarity
Metal bindingi283 – 2831ZincBy similarity
Binding sitei518 – 5181Glutamate
Sitei614 – 6141Functional determinant of NMDA receptorsBy similarity
Binding sitei731 – 7311Glutamate; via amide nitrogen

GO - Molecular functioni

  • ATPase binding Source: RGD
  • cell adhesion molecule binding Source: RGD
  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • glutamate binding Source: UniProtKB
  • glutamate receptor binding Source: RGD
  • ionotropic glutamate receptor activity Source: RGD
  • neurotransmitter binding Source: RGD
  • NMDA glutamate receptor activity Source: RGD
  • protein complex binding Source: RGD
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • receptor binding Source: RGD
  • scaffold protein binding Source: BHF-UCL
  • voltage-gated cation channel activity Source: RGD
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • action potential Source: RGD
  • cellular response to amino acid stimulus Source: RGD
  • cellular response to dsRNA Source: RGD
  • cellular response to growth factor stimulus Source: RGD
  • cellular response to lipid Source: RGD
  • cellular response to magnesium ion Source: RGD
  • cellular response to manganese ion Source: RGD
  • cellular response to zinc ion Source: RGD
  • cerebral cortex development Source: RGD
  • excitatory postsynaptic potential Source: RGD
  • hippocampus development Source: RGD
  • ionotropic glutamate receptor signaling pathway Source: RGD
  • memory Source: UniProtKB
  • positive regulation of cell death Source: RGD
  • positive regulation of excitatory postsynaptic potential Source: BHF-UCL
  • protein tetramerization Source: RGD
  • regulation of long-term neuronal synaptic plasticity Source: RGD
  • response to amine Source: RGD
  • response to ammonium ion Source: RGD
  • response to calcium ion Source: RGD
  • response to carbohydrate Source: RGD
  • response to cocaine Source: RGD
  • response to drug Source: RGD
  • response to ethanol Source: RGD
  • response to fungicide Source: RGD
  • response to light stimulus Source: RGD
  • response to manganese ion Source: RGD
  • response to methylmercury Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to other organism Source: RGD
  • rhythmic process Source: RGD
  • spinal cord development Source: RGD
  • synaptic transmission Source: RGD
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 2A
Short name:
GluN2A
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-1
N-methyl D-aspartate receptor subtype 2A
Short name:
NMDAR2A
Short name:
NR2A
Gene namesi
Name:Grin2a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2737. Grin2a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 555533ExtracellularSequence analysisAdd
BLAST
Transmembranei556 – 57621HelicalSequence analysisAdd
BLAST
Topological domaini577 – 63357CytoplasmicSequence analysisAdd
BLAST
Transmembranei634 – 65421HelicalSequence analysisAdd
BLAST
Topological domaini655 – 816162ExtracellularSequence analysisAdd
BLAST
Transmembranei817 – 83721HelicalSequence analysisAdd
BLAST
Topological domaini838 – 1464627CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • dendritic spine Source: MGI
  • neuron projection Source: UniProtKB
  • NMDA selective glutamate receptor complex Source: UniProtKB
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: UniProtKB-SubCell
  • presynaptic membrane Source: UniProtKB
  • synapse Source: UniProtKB
  • terminal bouton Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2096669.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 14641442Glutamate receptor ionotropic, NMDA 2APRO_0000011576Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence analysis
Disulfide bondi87 ↔ 320By similarity
Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence analysis
Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence analysis
Glycosylationi444 – 4441N-linked (GlcNAc...)Sequence analysis
Glycosylationi541 – 5411N-linked (GlcNAc...)Sequence analysis
Modified residuei882 – 8821PhosphoserineCombined sources
Modified residuei890 – 8901PhosphoserineCombined sources
Modified residuei929 – 9291PhosphoserineCombined sources
Modified residuei1025 – 10251PhosphoserineCombined sources
Modified residuei1059 – 10591PhosphoserineCombined sources
Modified residuei1062 – 10621PhosphoserineCombined sources
Modified residuei1198 – 11981PhosphoserineCombined sources
Modified residuei1291 – 12911PhosphoserineCombined sources

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ00959.
PRIDEiQ00959.

PTM databases

iPTMnetiQ00959.
PhosphoSiteiQ00959.
SwissPalmiQ00959.
UniCarbKBiQ00959.

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. Interacts with AIP1. Found in a complex with GRIN1 and GRIN3B. Interacts with HIP1 and NETO1. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes (By similarity). Interacts with PDZ domains of INADL and DLG4. Interacts with LRFN2.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg4P310165EBI-630970,EBI-375655
SrcP054805EBI-630970,EBI-298680From a different organism.

GO - Molecular functioni

  • ATPase binding Source: RGD
  • cell adhesion molecule binding Source: RGD
  • glutamate receptor binding Source: RGD
  • protein complex binding Source: RGD
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • receptor binding Source: RGD
  • scaffold protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi246574. 6 interactions.
DIPiDIP-34031N.
IntActiQ00959. 5 interactions.
MINTiMINT-93314.
STRINGi10116.ENSRNOP00000042235.

Chemistry

BindingDBiQ00959.

Structurei

Secondary structure

1
1464
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi406 – 4105Combined sources
Turni414 – 4163Combined sources
Beta strandi417 – 4215Combined sources
Turni424 – 4263Combined sources
Beta strandi434 – 44714Combined sources
Beta strandi449 – 45810Combined sources
Helixi459 – 47113Combined sources
Beta strandi475 – 4795Combined sources
Beta strandi482 – 4854Combined sources
Helixi495 – 5017Combined sources
Beta strandi506 – 5083Combined sources
Helixi516 – 5194Combined sources
Beta strandi522 – 5243Combined sources
Beta strandi529 – 5313Combined sources
Beta strandi533 – 5386Combined sources
Helixi668 – 6714Combined sources
Helixi673 – 6753Combined sources
Beta strandi676 – 6783Combined sources
Helixi689 – 6979Combined sources
Helixi699 – 7057Combined sources
Helixi706 – 7083Combined sources
Helixi713 – 7219Combined sources
Beta strandi726 – 7316Combined sources
Helixi732 – 7409Combined sources
Beta strandi747 – 7515Combined sources
Helixi752 – 7543Combined sources
Helixi755 – 7573Combined sources
Beta strandi759 – 7613Combined sources
Beta strandi764 – 7663Combined sources
Helixi772 – 78413Combined sources
Helixi787 – 7959Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A5SX-ray1.70A401-539[»]
2A5TX-ray2.00B401-539[»]
4JWXX-ray1.50A404-801[»]
4NF4X-ray2.00B402-539[»]
B661-802[»]
4NF5X-ray1.90B402-539[»]
B661-802[»]
4NF6X-ray2.10B402-539[»]
B661-802[»]
4NF8X-ray1.86B402-539[»]
B661-802[»]
ProteinModelPortaliQ00959.
SMRiQ00959. Positions 404-801.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00959.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni511 – 5133Glutamate binding
Regioni689 – 6902Glutamate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1462 – 14643PDZ-binding

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ00959.
KOiK05209.
PhylomeDBiQ00959.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR018884. NMDAR2_C.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
PF10565. NMDAR2_C. 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.

Q00959-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRLGYWTLL VLPALLVWRD PAQNAAAEKG PPALNIAVLL GHSHDVTERE
60 70 80 90 100
LRNLWGPEQA TGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF
110 120 130 140 150
GDDTDQEAVA QMLDFISSQT FIPILGIHGG ASMIMADKDP TSTFFQFGAS
160 170 180 190 200
IQQQATVMLK IMQDYDWHVF SLVTTIFPGY RDFISFIKTT VDNSFVGWDM
210 220 230 240 250
QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL SEARSLGLTG
260 270 280 290 300
YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGLGILT
310 320 330 340 350
TAASSMLEKF SYIPEAKASC YGQAEKPETP LHTLHQFMVN VTWDGKDLSF
360 370 380 390 400
TEEGYQVHPR LVVIVLNKDR EWEKVGKWEN QTLSLRHAVW PRYKSFSDCE
410 420 430 440 450
PDDNHLSIVT LEEAPFVIVE DIDPLTETCV RNTVPCRKFV KINNSTNEGM
460 470 480 490 500
NVKKCCKGFC IDILKKLSRT VKFTYDLYLV TNGKHGKKVN NVWNGMIGEV
510 520 530 540 550
VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS NGTVSPSAFL
560 570 580 590 600
EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT
610 620 630 640 650
IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA
660 670 680 690 700
AFMIQEEFVD QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY
710 720 730 740 750
MHQYMTRFNQ RGVEDALVSL KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI
760 770 780 790 800
GSGYIFASTG YGIALQKGSP WKRQIDLALL QFVGDGEMEE LETLWLTGIC
810 820 830 840 850
HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL FYWKLRFCFT
860 870 880 890 900
GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS
910 920 930 940 950
AKNISNMSNM NSSRMDSPKR ATDFIQRGSL IVDMVSDKGN LIYSDNRSFQ
960 970 980 990 1000
GKDSIFGDNM NELQTFVANR HKDNLSNYVF QGQHPLTLNE SNPNTVEVAV
1010 1020 1030 1040 1050
STESKGNSRP RQLWKKSMES LRQDSLNQNP VSQRDEKTAE NRTHSLKSPR
1060 1070 1080 1090 1100
YLPEEVAHSD ISETSSRATC HREPDNNKNH KTKDNFKRSM ASKYPKDCSD
1110 1120 1130 1140 1150
VDRTYMKTKA SSPRDKIYTI DGEKEPSFHL DPPQFVENIT LPENVGFPDT
1160 1170 1180 1190 1200
YQDHNENFRK GDSTLPMNRN PLHNEDGLPN NDQYKLYAKH FTLKDKGSPH
1210 1220 1230 1240 1250
SEGSDRYRQN STHCRSCLSN LPTYSGHFTM RSPFKCDACL RMGNLYDIDE
1260 1270 1280 1290 1300
DQMLQETGNP ATREEVYQQD WSQNNALQFQ KNKLRINRQH SYDNILDKPR
1310 1320 1330 1340 1350
EIDLSRPSRS ISLKDRERLL EGNLYGSLFS VPSSKLLGNK SSLFPQGLED
1360 1370 1380 1390 1400
SKRSKSLLPD HASDNPFLHT YGDDQRLVIG RCPSDPYKHS LPSQAVNDSY
1410 1420 1430 1440 1450
LRSSLRSTAS YCSRDSRGHS DVYISEHVMP YAANKNTMYS TPRVLNSCSN
1460
RRVYKKMPSI ESDV
Length:1,464
Mass (Da):165,469
Last modified:December 15, 1998 - v2
Checksum:iDC1528E1898DECA4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti246 – 2461L → F in BAA02498 (PubMed:8428958).Curated
Sequence conflicti758 – 7581S → T in BAA02498 (PubMed:8428958).Curated
Sequence conflicti758 – 7581S → T in AAB58801 (Ref. 4) Curated
Sequence conflicti990 – 9901E → D in AAB58801 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91561 mRNA. Translation: AAC03565.1.
D13211 mRNA. Translation: BAA02498.1.
AF001423 mRNA. Translation: AAB58801.1.
PIRiA43274.
RefSeqiNP_036705.3. NM_012573.3.
UniGeneiRn.9710.

Genome annotation databases

GeneIDi24409.
KEGGirno:24409.
UCSCiRGD:2737. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91561 mRNA. Translation: AAC03565.1.
D13211 mRNA. Translation: BAA02498.1.
AF001423 mRNA. Translation: AAB58801.1.
PIRiA43274.
RefSeqiNP_036705.3. NM_012573.3.
UniGeneiRn.9710.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A5SX-ray1.70A401-539[»]
2A5TX-ray2.00B401-539[»]
4JWXX-ray1.50A404-801[»]
4NF4X-ray2.00B402-539[»]
B661-802[»]
4NF5X-ray1.90B402-539[»]
B661-802[»]
4NF6X-ray2.10B402-539[»]
B661-802[»]
4NF8X-ray1.86B402-539[»]
B661-802[»]
ProteinModelPortaliQ00959.
SMRiQ00959. Positions 404-801.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246574. 6 interactions.
DIPiDIP-34031N.
IntActiQ00959. 5 interactions.
MINTiMINT-93314.
STRINGi10116.ENSRNOP00000042235.

Chemistry

BindingDBiQ00959.
ChEMBLiCHEMBL2096669.

Protein family/group databases

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

PTM databases

iPTMnetiQ00959.
PhosphoSiteiQ00959.
SwissPalmiQ00959.
UniCarbKBiQ00959.

Proteomic databases

PaxDbiQ00959.
PRIDEiQ00959.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24409.
KEGGirno:24409.
UCSCiRGD:2737. rat.

Organism-specific databases

CTDi2903.
RGDi2737. Grin2a.

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ00959.
KOiK05209.
PhylomeDBiQ00959.

Miscellaneous databases

EvolutionaryTraceiQ00959.
PROiQ00959.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR018884. NMDAR2_C.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
PF10565. NMDAR2_C. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H., Burnashev N., Sakmann B., Seeburg P.H.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 595 AND 597-598.
  3. "Molecular characterization of the family of the N-methyl-D-aspartate receptor subunits."
    Ishii T., Moriyoshi K., Sugihara H., Sakurada K., Kadotani H., Yokoi M., Akazawa C., Shigemoto R., Mizuno N., Masu M., Nakanishi S.
    J. Biol. Chem. 268:2836-2843(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Forebrain.
  4. "Nucleotide sequence of rat NMDA receptor gene NMDAR2A."
    Boulter J.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  5. "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.
  6. "A novel multiple PDZ domain-containing molecule interacting with N-methyl-d-aspartate receptors and neuronal cell adhesion proteins."
    Hirao K., Hata Y., Ide N., Takeuchi M., Irie M., Yao I., Deguchi M., Toyoda A., Suedhof T.C., Takai Y.
    J. Biol. Chem. 273:21105-21110(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AIP1.
  7. "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.
  8. "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: SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
  9. "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.
  10. "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.
  11. "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.
  12. "A novel family of adhesion-like molecules that interacts with the NMDA receptor."
    Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J.
    J. Neurosci. 26:2174-2183(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRFN2.
  13. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929; SER-1025; SER-1059; SER-1062; SER-1198 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Subunit arrangement and function in NMDA receptors."
    Furukawa H., Singh S.K., Mancusso R., Gouaux E.
    Nature 438:185-192(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 401-802 IN COMPLEXES WITH GRIN1 AND GLUTAMATE.

Entry informationi

Entry nameiNMDE1_RAT
AccessioniPrimary (citable) accession number: Q00959
Secondary accession number(s): O08948, Q63728
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 15, 1998
Last modified: July 6, 2016
This is version 156 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.