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Protein

Glutamate receptor ionotropic, NMDA 1

Gene

Grin1

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. Mediated by glycine. Plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei523 – 5231Glycine1 Publication
Binding sitei688 – 6881Glycine1 Publication
Binding sitei732 – 7321Glycine1 Publication

GO - Molecular functioni

  • calcium channel activity Source: Ensembl
  • calcium ion binding Source: Ensembl
  • enzyme binding Source: RGD
  • extracellular-glutamate-gated ion channel activity Source: GO_Central
  • glutamate binding Source: UniProtKB
  • glutamate receptor binding Source: RGD
  • glycine binding Source: UniProtKB
  • ionotropic glutamate receptor activity Source: RGD
  • neurotransmitter binding Source: RGD
  • N-methyl-D-aspartate selective glutamate receptor activity Source: RGD
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • receptor binding Source: RGD
  • voltage-gated cation channel activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Calcium, Magnesium

Enzyme and pathway databases

ReactomeiREACT_272967. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_276289. CREB phosphorylation through the activation of CaMKII.
REACT_277188. EPHB-mediated forward signaling.
REACT_338101. Unblocking of NMDA receptor, glutamate binding and activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, NMDA 1
Short name:
GluN1
Alternative name(s):
Glutamate [NMDA] receptor subunit zeta-1
N-methyl-D-aspartate receptor subunit NR1
Short name:
NMD-R1
Gene namesi
Name:Grin1
Synonyms:Nmdar1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi2736. Grin1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 559541ExtracellularSequence AnalysisAdd
BLAST
Transmembranei560 – 58021HelicalSequence AnalysisAdd
BLAST
Topological domaini581 – 63656CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei637 – 65721HelicalSequence AnalysisAdd
BLAST
Topological domaini658 – 812155ExtracellularSequence AnalysisAdd
BLAST
Transmembranei813 – 83321HelicalSequence AnalysisAdd
BLAST
Topological domaini834 – 938105CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cell surface Source: Ensembl
  • dendrite Source: GO_Central
  • dendrite membrane Source: BHF-UCL
  • dendritic branch Source: RGD
  • dendritic spine Source: RGD
  • endoplasmic reticulum Source: Ensembl
  • excitatory synapse Source: BHF-UCL
  • neuronal cell body Source: RGD
  • neuronal postsynaptic density Source: Ensembl
  • N-methyl-D-aspartate selective glutamate receptor complex Source: RGD
  • plasma membrane Source: GO_Central
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: GO_Central
  • synapse Source: MGI
  • synaptic cleft Source: RGD
  • synaptic vesicle Source: Ensembl
  • terminal bouton Source: RGD
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 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 938920Glutamate receptor ionotropic, NMDA 1PRO_0000011589Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi79 – 79InterchainBy similarity
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis
Modified residuei889 – 8891Phosphoserine; by PKCBy similarity
Modified residuei890 – 8901Phosphoserine; by PKC1 Publication
Modified residuei896 – 8961Phosphoserine; by PKCBy similarity
Modified residuei897 – 8971Phosphoserine; by PKC1 Publication

Post-translational modificationi

NMDA is probably regulated by C-terminal phosphorylation of an isoform of NR1 by PKC. Dephosphorylated on Ser-897 probably by protein phosphatase 2A (PPP2CB). Its phosphorylated state is influenced by the formation of the NMDAR-PPP2CB complex and the NMDAR channel activity.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP35439.
PRIDEiP35439.

PTM databases

PhosphoSiteiP35439.

Expressioni

Gene expression databases

ExpressionAtlasiP35439. baseline and differential.
GenevisibleiP35439. RN.

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); disulfide-linked (By similarity). Found in a complex with GRIN2A or GRIN2B, GRIN3A and PPP2CB. Found in a complex with GRIN2A or GRIN2B and GRIN3B. 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 DLG4 and MPDZ. Interacts with LRFN1 and LRFN2. Interacts with MYZAP.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg4P310164EBI-877897,EBI-375655
Lrfn2Q460M52EBI-877897,EBI-877185
Lrfn2Q80TG92EBI-877935,EBI-877092From a different organism.
Pdzk1Q9JJ403EBI-877897,EBI-7713572

Protein-protein interaction databases

BioGridi246573. 7 interactions.
DIPiDIP-674N.
IntActiP35439. 12 interactions.
MINTiMINT-101336.
STRINGi10116.ENSRNOP00000029227.

Structurei

Secondary structure

1
938
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 3510Combined sources
Helixi36 – 5015Combined sources
Beta strandi59 – 668Combined sources
Helixi71 – 8010Combined sources
Helixi83 – 853Combined sources
Beta strandi87 – 926Combined sources
Turni98 – 1036Combined sources
Helixi104 – 1129Combined sources
Turni113 – 1153Combined sources
Beta strandi118 – 1225Combined sources
Helixi126 – 1294Combined sources
Turni131 – 1333Combined sources
Beta strandi137 – 1415Combined sources
Helixi144 – 1463Combined sources
Helixi147 – 15610Combined sources
Helixi157 – 1593Combined sources
Beta strandi163 – 1708Combined sources
Helixi171 – 18515Combined sources
Turni186 – 1883Combined sources
Beta strandi192 – 1976Combined sources
Helixi205 – 2128Combined sources
Beta strandi218 – 2225Combined sources
Helixi225 – 23713Combined sources
Beta strandi246 – 2483Combined sources
Turni251 – 2544Combined sources
Turni256 – 2605Combined sources
Beta strandi267 – 2715Combined sources
Helixi277 – 29620Combined sources
Beta strandi298 – 3003Combined sources
Helixi317 – 32610Combined sources
Beta strandi334 – 3363Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi342 – 3443Combined sources
Beta strandi351 – 3577Combined sources
Beta strandi360 – 3634Combined sources
Beta strandi365 – 3673Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi398 – 4025Combined sources
Turni406 – 4083Combined sources
Beta strandi409 – 4135Combined sources
Beta strandi426 – 4283Combined sources
Beta strandi434 – 4396Combined sources
Beta strandi450 – 4578Combined sources
Helixi458 – 47013Combined sources
Beta strandi474 – 4785Combined sources
Beta strandi487 – 4893Combined sources
Beta strandi491 – 4944Combined sources
Beta strandi496 – 4983Combined sources
Helixi500 – 5067Combined sources
Beta strandi511 – 5133Combined sources
Helixi521 – 5244Combined sources
Beta strandi527 – 5293Combined sources
Beta strandi533 – 54311Combined sources
Helixi670 – 6734Combined sources
Beta strandi684 – 6874Combined sources
Helixi688 – 6947Combined sources
Helixi697 – 6993Combined sources
Helixi700 – 7067Combined sources
Turni707 – 7093Combined sources
Beta strandi711 – 7133Combined sources
Helixi714 – 7229Combined sources
Beta strandi727 – 7326Combined sources
Helixi733 – 74210Combined sources
Beta strandi746 – 7483Combined sources
Beta strandi753 – 7586Combined sources
Beta strandi761 – 7633Combined sources
Helixi769 – 78113Combined sources
Helixi784 – 7929Combined sources
Beta strandi794 – 7963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PB7X-ray1.35A394-544[»]
A663-800[»]
1PB8X-ray1.45A394-544[»]
A663-800[»]
1PB9X-ray1.60A394-544[»]
A663-800[»]
1PBQX-ray1.90A/B394-800[»]
1Y1MX-ray1.80A/B394-544[»]
A/B663-800[»]
1Y1ZX-ray1.50A394-544[»]
A663-800[»]
1Y20X-ray1.40A394-544[»]
A663-800[»]
2A5TX-ray2.00A394-544[»]
3Q41X-ray3.40A/B/C21-393[»]
4KCCX-ray1.89A394-544[»]
A663-800[»]
4KFQX-ray2.20A/B394-544[»]
A/B663-800[»]
4NF4X-ray2.00A394-544[»]
A663-800[»]
4NF5X-ray1.90A394-544[»]
A663-800[»]
4NF6X-ray2.10A394-544[»]
A663-800[»]
4NF8X-ray1.86A394-544[»]
A663-800[»]
4PE5X-ray3.96A/C23-847[»]
ProteinModelPortaliP35439.
SMRiP35439. Positions 396-800.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35439.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni516 – 5183Glycine binding

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG282132.
GeneTreeiENSGT00760000119186.
HOGENOMiHOG000231491.
HOVERGENiHBG052638.
InParanoidiP35439.
KOiK05208.
OMAiTMSDGTC.
OrthoDBiEOG79GT5V.
PhylomeDBiP35439.
TreeFamiTF351405.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR018882. CaM-bd_C0_NMDA_rcpt_NR1.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF10562. CaM_bdg_C0. 1 hit.
PF00060. Lig_chan. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequences (7)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P35439-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN
60 70 80 90 100
KRHGSWKIQL NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND
110 120 130 140 150
HFTPTPVSYT AGFYRIPVLG LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV
160 170 180 190 200
WFEMMRVYNW NHIILLVSDD HEGRAAQKRL ETLLEERESK AEKVLQFDPG
210 220 230 240 250
TKNVTALLME ARELEARVII LSASEDDAAT VYRAAAMLNM TGSGYVWLVG
260 270 280 290 300
EREISGNALR YAPDGIIGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN
310 320 330 340 350
ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN
360 370 380 390 400
YSIMNLQNRK LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI
410 420 430 440 450
VTIHQEPFVY VKPTMSDGTC KEEFTVNGDP VKKVICTGPN DTSPGSPRHT
460 470 480 490 500
VPQCCYGFCI DLLIKLARTM NFTYEVHLVA DGKFGTQERV NNSNKKEWNG
510 520 530 540 550
MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI LVKKEIPRST
560 570 580 590 600
LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA
610 620 630 640 650
LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN
660 670 680 690 700
LAAFLVLDRP EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS
710 720 730 740 750
TMYRHMEKHN YESAAEAIQA VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG
760 770 780 790 800
ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH ENGFMEDLDK TWVRYQECDS
810 820 830 840 850
RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH KDARRKQMQL
860 870 880 890 900
AFAAVNVWRK NLQDRKSGRA EPDPKKKATF RAITSTLASS FKRRRSSKDT
910 920 930
STGGGRGALQ NQKDTVLPRR AIEREEGQLQ LCSRHRES
Length:938
Mass (Da):105,509
Last modified:June 1, 1994 - v1
Checksum:i613D36E38F05BC73
GO
Isoform B (identifier: P35439-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK

Show »
Length:959
Mass (Da):108,045
Checksum:iD965531F6C38EDDD
GO
Isoform C (identifier: P35439-3) [UniParc]FASTAAdd to basket

Also known as: NMDAR1-2a subunit

The sequence of this isoform differs from the canonical sequence as follows:
     864-900: Missing.

Show »
Length:901
Mass (Da):101,345
Checksum:iA320F3585664F652
GO
Isoform D (identifier: P35439-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     901-938: STGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES → QYHPTDITGPLNLSDPSVSTVV

Show »
Length:922
Mass (Da):103,615
Checksum:iE31E00296E49D08D
GO
Isoform E (identifier: P35439-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     864-885: DRKSGRAEPDPKKKATFRAITS → QYHPTDITGPLNLSDPSVSTVV
     886-938: Missing.

Show »
Length:885
Mass (Da):99,451
Checksum:i6DAA83EFC08C30D8
GO
Isoform F (identifier: P35439-6) [UniParc]FASTAAdd to basket

Also known as: NMDAR1-2b subunit

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK
     864-900: Missing.

Show »
Length:922
Mass (Da):103,881
Checksum:i847CEED410182B5C
GO
Isoform G (identifier: P35439-7) [UniParc]FASTAAdd to basket

Also known as: NMDAR1-4b subunit

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK
     864-885: DRKSGRAEPDPKKKATFRAITS → QYHPTDITGPLNLSDPSVSTVV
     886-938: Missing.

Show »
Length:906
Mass (Da):101,987
Checksum:i1872055038F790FF
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei190 – 1901K → KSKKRNYENLDQLSYDNKRG PK in isoform B, isoform F and isoform G. CuratedVSP_000140
Alternative sequencei864 – 90037Missing in isoform F and isoform C. CuratedVSP_000141Add
BLAST
Alternative sequencei864 – 88522DRKSG…RAITS → QYHPTDITGPLNLSDPSVST VV in isoform E and isoform G. CuratedVSP_000142Add
BLAST
Alternative sequencei886 – 93853Missing in isoform E and isoform G. CuratedVSP_000143Add
BLAST
Alternative sequencei901 – 93838STGGG…RHRES → QYHPTDITGPLNLSDPSVST VV in isoform D. CuratedVSP_000144Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63255 mRNA. Translation: CAA44914.1.
AY157515 Genomic DNA. Translation: AAA16366.1.
U08261 mRNA. Translation: AAB50926.1.
U08262 mRNA. Translation: AAB50927.1.
U08263 mRNA. Translation: AAB50928.1.
U08264 mRNA. Translation: AAB50929.1.
U08265 mRNA. Translation: AAB50930.1.
U08267 mRNA. Translation: AAB50932.1.
U08268 mRNA. Translation: AAB50933.1.
S39217 mRNA. Translation: AAB22431.1.
S39218 mRNA. Translation: AAB22432.1.
S39219 mRNA. Translation: AAB22433.1.
S39220 mRNA. Translation: AAB22434.1.
S39221 mRNA. Translation: AAB22435.1.
X65227 mRNA. Translation: CAA46335.1.
PIRiJN0336.
JN0337.
JN0338.
JN0339.
JN0340.
JN0341.
JN0342.
S19710.
RefSeqiNP_001257531.1. NM_001270602.1. [P35439-2]
NP_001257532.1. NM_001270603.1. [P35439-6]
NP_001257534.1. NM_001270605.1. [P35439-3]
NP_001257537.1. NM_001270608.1. [P35439-7]
NP_001257539.1. NM_001270610.1. [P35439-5]
NP_001274352.1. NM_001287423.1. [P35439-4]
NP_058706.1. NM_017010.2. [P35439-1]
UniGeneiRn.9840.

Genome annotation databases

EnsembliENSRNOT00000037725; ENSRNOP00000029227; ENSRNOG00000011726. [P35439-2]
ENSRNOT00000044246; ENSRNOP00000043301; ENSRNOG00000011726. [P35439-6]
ENSRNOT00000049297; ENSRNOP00000049198; ENSRNOG00000011726. [P35439-1]
GeneIDi24408.
KEGGirno:24408.
UCSCiRGD:2736. rat. [P35439-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63255 mRNA. Translation: CAA44914.1.
AY157515 Genomic DNA. Translation: AAA16366.1.
U08261 mRNA. Translation: AAB50926.1.
U08262 mRNA. Translation: AAB50927.1.
U08263 mRNA. Translation: AAB50928.1.
U08264 mRNA. Translation: AAB50929.1.
U08265 mRNA. Translation: AAB50930.1.
U08267 mRNA. Translation: AAB50932.1.
U08268 mRNA. Translation: AAB50933.1.
S39217 mRNA. Translation: AAB22431.1.
S39218 mRNA. Translation: AAB22432.1.
S39219 mRNA. Translation: AAB22433.1.
S39220 mRNA. Translation: AAB22434.1.
S39221 mRNA. Translation: AAB22435.1.
X65227 mRNA. Translation: CAA46335.1.
PIRiJN0336.
JN0337.
JN0338.
JN0339.
JN0340.
JN0341.
JN0342.
S19710.
RefSeqiNP_001257531.1. NM_001270602.1. [P35439-2]
NP_001257532.1. NM_001270603.1. [P35439-6]
NP_001257534.1. NM_001270605.1. [P35439-3]
NP_001257537.1. NM_001270608.1. [P35439-7]
NP_001257539.1. NM_001270610.1. [P35439-5]
NP_001274352.1. NM_001287423.1. [P35439-4]
NP_058706.1. NM_017010.2. [P35439-1]
UniGeneiRn.9840.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PB7X-ray1.35A394-544[»]
A663-800[»]
1PB8X-ray1.45A394-544[»]
A663-800[»]
1PB9X-ray1.60A394-544[»]
A663-800[»]
1PBQX-ray1.90A/B394-800[»]
1Y1MX-ray1.80A/B394-544[»]
A/B663-800[»]
1Y1ZX-ray1.50A394-544[»]
A663-800[»]
1Y20X-ray1.40A394-544[»]
A663-800[»]
2A5TX-ray2.00A394-544[»]
3Q41X-ray3.40A/B/C21-393[»]
4KCCX-ray1.89A394-544[»]
A663-800[»]
4KFQX-ray2.20A/B394-544[»]
A/B663-800[»]
4NF4X-ray2.00A394-544[»]
A663-800[»]
4NF5X-ray1.90A394-544[»]
A663-800[»]
4NF6X-ray2.10A394-544[»]
A663-800[»]
4NF8X-ray1.86A394-544[»]
A663-800[»]
4PE5X-ray3.96A/C23-847[»]
ProteinModelPortaliP35439.
SMRiP35439. Positions 396-800.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246573. 7 interactions.
DIPiDIP-674N.
IntActiP35439. 12 interactions.
MINTiMINT-101336.
STRINGi10116.ENSRNOP00000029227.

Chemistry

BindingDBiP35439.
ChEMBLiCHEMBL2096911.
GuidetoPHARMACOLOGYi455.

PTM databases

PhosphoSiteiP35439.

Proteomic databases

PaxDbiP35439.
PRIDEiP35439.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000037725; ENSRNOP00000029227; ENSRNOG00000011726. [P35439-2]
ENSRNOT00000044246; ENSRNOP00000043301; ENSRNOG00000011726. [P35439-6]
ENSRNOT00000049297; ENSRNOP00000049198; ENSRNOG00000011726. [P35439-1]
GeneIDi24408.
KEGGirno:24408.
UCSCiRGD:2736. rat. [P35439-1]

Organism-specific databases

CTDi2902.
RGDi2736. Grin1.

Phylogenomic databases

eggNOGiNOG282132.
GeneTreeiENSGT00760000119186.
HOGENOMiHOG000231491.
HOVERGENiHBG052638.
InParanoidiP35439.
KOiK05208.
OMAiTMSDGTC.
OrthoDBiEOG79GT5V.
PhylomeDBiP35439.
TreeFamiTF351405.

Enzyme and pathway databases

ReactomeiREACT_272967. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_276289. CREB phosphorylation through the activation of CaMKII.
REACT_277188. EPHB-mediated forward signaling.
REACT_338101. Unblocking of NMDA receptor, glutamate binding and activation.

Miscellaneous databases

EvolutionaryTraceiP35439.
NextBioi603223.
PROiP35439.

Gene expression databases

ExpressionAtlasiP35439. baseline and differential.
GenevisibleiP35439. RN.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR018882. CaM-bd_C0_NMDA_rcpt_NR1.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF10562. CaM_bdg_C0. 1 hit.
PF00060. Lig_chan. 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

  1. "Molecular cloning and characterization of the rat NMDA receptor."
    Moriyoshi K., Masu M., Ishii T., Shigemoto R., Mizuno N., Nakanishi S.
    Nature 354:31-37(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Brain.
  2. "Alternative splicing generates functionally distinct N-methyl-D-aspartate receptors."
    Nakanishi N., Axel R., Shneider N.A.
    Proc. Natl. Acad. Sci. U.S.A. 89:8552-8556(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor."
    Hollmann M., Boulter J., Maron C., Beasley L., Sullivan J., Pecht G., Heinemann S.F.
    Neuron 10:943-954(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Forebrain.
  4. "Cloning and analysis of the 5' flanking sequence of the rat N-methyl-D-aspartate receptor 1 (NMDAR1) gene."
    Bai G., Kusiak J.W.
    Biochim. Biophys. Acta 1152:197-200(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-86.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  5. "Structures and properties of seven isoforms of the NMDA receptor generated by alternative splicing."
    Sugihara H., Moriyoshi K., Ishii T., Masu M., Nakanishi S.
    Biochem. Biophys. Res. Commun. 185:826-832(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
    Tissue: Brain.
  6. "Combinatorial RNA splicing alters the surface charge on the NMDA receptor."
    Anantharam V., Panchal R., Wilson A., Koltchin V.V., Treistman S.N., Bayley H.
    FEBS Lett. 305:27-30(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
    Tissue: Brain.
  7. "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: PHOSPHORYLATION AT SER-897, DEPHOSPHORYLATION BY PPP2CB, IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B; GRIN3A AND PPP2CB.
  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: CHARACTERIZATION, IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3A.
  9. "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 GRIN2A OR GRIN2B AND GRIN3A.
  10. "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 GRIN2A OR GRIN2B AND GRIN3A.
  11. "SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation."
    Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.
    Neuron 43:563-574(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MPDZ AND DLG4.
  12. "Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially phosphorylated by protein kinase C isoforms."
    Sanchez-Perez A.M., Felipo V.
    Neurochem. Int. 47:84-91(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-890.
  13. "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.
  14. "SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses."
    Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., Kim E.
    Neuron 50:233-245(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRFN1.
  15. "GRINL1A colocalizes with N-methyl D-aspartate receptor NR1 subunit and reduces N-methyl D-aspartate toxicity."
    Roginski R.S., Goubaeva F., Mikami M., Fried-Cassorla E., Nair M.R., Yang J.
    NeuroReport 19:1721-1726(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYZAP.
  16. "Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core."
    Furukawa H., Gouaux E.
    EMBO J. 22:2873-2885(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 394-800 IN COMPLEXES WITH AGONISTS AND ANTAGONIST.
  17. "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 (2.0 ANGSTROMS) OF 394-800 IN COMPLEX WITH GRIN2A; GLYCINE AND GLUTAMATE, SUBUNIT.
  18. "Mechanism of partial agonist action at the NR1 subunit of NMDA receptors."
    Inanobe A., Furukawa H., Gouaux E.
    Neuron 47:71-84(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 394-800 IN COMPLEXES WITH AGONISTS, FUNCTION.

Entry informationi

Entry nameiNMDZ1_RAT
AccessioniPrimary (citable) accession number: P35439
Secondary accession number(s): Q62646
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 24, 2015
This is version 172 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

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 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.