Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q05586 (NMDZ1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GRIN1
Synonyms:NMDAR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length938 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein 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 By similarity.

Subunit structure

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. Found in a complex with GRIN2A or GRIN2B, GRIN3A or GRIN3B and PPP2CB. Interacts with DLG4 and MPDZ. 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 LRFN1 and LRFN2 By similarity. Interacts with MYZAP. Ref.10 Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Cell junctionsynapsepostsynaptic cell membrane By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Note: Enriched in postsynaptic plasma membrane and postsynaptic densities By similarity.

Post-translational modification

NMDA is probably regulated by C-terminal phosphorylation of an isoform ofNR1 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. Ref.9

Involvement in disease

Mental retardation, autosomal dominant 8 (MRD8) [MIM:614254]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR1/GRIN1 subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Mental retardation
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCalcium
Magnesium
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

calcium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cation transport

Inferred from direct assay Ref.3. Source: UniProtKB

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular response to manganese ion

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

conditioned taste aversion

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

ionotropic glutamate receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

long-term memory

Inferred from electronic annotation. Source: Ensembl

male mating behavior

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

olfactory learning

Inferred from electronic annotation. Source: Ensembl

pons maturation

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of excitatory postsynaptic membrane potential

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

prepulse inhibition

Inferred from electronic annotation. Source: Ensembl

propylene metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

protein tetramerization

Inferred from electronic annotation. Source: Ensembl

regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of excitatory postsynaptic membrane potential

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of long-term neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of membrane potential

Inferred from direct assay PubMed 17047094Ref.2Ref.3. Source: UniProtKB

regulation of respiratory gaseous exchange

Inferred from electronic annotation. Source: Ensembl

regulation of synapse assembly

Inferred from electronic annotation. Source: Ensembl

respiratory gaseous exchange

Inferred from electronic annotation. Source: Ensembl

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from direct assay PubMed 18445116. Source: UniProtKB

response to fungicide

Inferred from electronic annotation. Source: Ensembl

response to morphine

Inferred from electronic annotation. Source: Ensembl

rhythmic process

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

social behavior

Inferred from electronic annotation. Source: Ensembl

suckling behavior

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Traceable author statement. Source: Reactome

synaptic transmission, glutamatergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

visual learning

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentN-methyl-D-aspartate selective glutamate receptor complex

Inferred from direct assay PubMed 10480938PubMed 17047094Ref.2. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from sequence or structural similarity. Source: BHF-UCL

dendrite

Inferred from direct assay PubMed 10749211. Source: UniProtKB

dendrite membrane

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from sequence or structural similarity. Source: BHF-UCL

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

excitatory synapse

Inferred from sequence or structural similarity. Source: BHF-UCL

integral component of plasma membrane

Inferred from direct assay Ref.3. Source: UniProtKB

neuron projection

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic density

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic membrane

Inferred from sequence or structural similarity. Source: UniProtKB

synapse

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic cleft

Inferred from sequence or structural similarity. Source: BHF-UCL

synaptic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

terminal bouton

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionN-methyl-D-aspartate selective glutamate receptor activity

Inferred from electronic annotation. Source: Ensembl

calcium channel activity

Inferred from electronic annotation. Source: Ensembl

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

calmodulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

glutamate binding

Inferred from direct assay Ref.3. Source: UniProtKB

glycine binding

Inferred from direct assay Ref.3. Source: UniProtKB

neurotransmitter binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 11937501. Source: IntAct

voltage-gated cation channel activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dlg3Q629363EBI-8286218,EBI-349596From a different organism.

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: Q05586-1)

Also known as: Long; NR1-3;

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.
Isoform 1 (identifier: Q05586-2)

Also known as: Short; NR1-1;

The sequence of this isoform differs from the canonical sequence as follows:
     864-885: DRKSGRAEPDPKKKATFRAITS → QYHPTDITGPLNLSDPSVSTVV
     886-938: Missing.
Isoform 2 (identifier: Q05586-3)

Also known as: Medium; NR1-2;

The sequence of this isoform differs from the canonical sequence as follows:
     864-900: Missing.
Isoform 4 (identifier: Q05586-4)

The sequence of this isoform differs from the canonical sequence as follows:
     901-922: STGGGRGALQNQKDTVLPRRAI → QYHPTDITGPLNLSDPSVSTVV
     923-938: Missing.
Isoform 5 (identifier: Q05586-5)

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK
Isoform 6 (identifier: Q05586-6)

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK
     901-922: STGGGRGALQNQKDTVLPRRAI → QYHPTDITGPLNLSDPSVSTVV
     923-938: Missing.
Isoform 7 (identifier: Q05586-7)

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK
     864-938: DRKSGRAEPD...LQLCSRHRES → QYHPTDITGPLNLSDPSVSTVV

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 938920Glutamate receptor ionotropic, NMDA 1
PRO_0000011587

Regions

Topological domain19 – 559541Extracellular Potential
Transmembrane560 – 58021Helical; Potential
Topological domain581 – 63656Cytoplasmic Potential
Transmembrane637 – 65721Helical; Potential
Topological domain658 – 812155Extracellular Potential
Transmembrane813 – 83321Helical; Potential
Topological domain834 – 938105Cytoplasmic Potential
Region516 – 5183Glycine binding By similarity

Sites

Binding site5231Glycine By similarity
Binding site6881Glycine By similarity
Binding site7321Glycine By similarity

Amino acid modifications

Modified residue8891Phosphoserine; by PKC Probable
Modified residue8901Phosphoserine; by PKC Probable
Modified residue8961Phosphoserine; by PKC Probable
Modified residue8971Phosphoserine; by PKC Probable
Glycosylation611N-linked (GlcNAc...) Potential
Glycosylation2031N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation2761N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential
Glycosylation4711N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential
Disulfide bond79Interchain Ref.10

Natural variations

Alternative sequence1901K → KSKKRNYENLDQLSYDNKRG PK in isoform 5, isoform 6 and isoform 7.
VSP_011777
Alternative sequence864 – 93875DRKSG…RHRES → QYHPTDITGPLNLSDPSVST VV in isoform 7.
VSP_045464
Alternative sequence864 – 90037Missing in isoform 2.
VSP_000139
Alternative sequence864 – 88522DRKSG…RAITS → QYHPTDITGPLNLSDPSVST VV in isoform 1.
VSP_000137
Alternative sequence886 – 93853Missing in isoform 1.
VSP_000138
Alternative sequence901 – 92222STGGG…PRRAI → QYHPTDITGPLNLSDPSVST VV in isoform 4 and isoform 6.
VSP_011778
Alternative sequence923 – 93816Missing in isoform 4 and isoform 6.
VSP_011779
Natural variant5401I → M. Ref.5
Corresponds to variant rs3181457 [ dbSNP | Ensembl ].
VAR_049187
Natural variant5601S → SS in MRD8; there is near abolition of the activity of the NMDA receptor in Xenopus oocytes; alters the 3-dimensional structure at the receptor's channel pore entrance. Ref.13
VAR_066597
Natural variant6621E → K in MRD8; this mutation produces a significant increase in NMDA receptor-induced calcium currents; excessive calcium influx through NMDA receptor could lead to excitotoxic neuronal cell damage. Ref.13
VAR_066598
Natural variant6821A → S. Ref.5
Corresponds to variant rs1126448 [ dbSNP | Ensembl ].
VAR_069057

Experimental info

Sequence conflict3891P → S in AAB25917. Ref.8
Sequence conflict4881E → K in AAB59361. Ref.1

Secondary structure

..... 938
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 (Long) (NR1-3) [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: CDF5402769E530AB

FASTA938105,373
        10         20         30         40         50         60 
MSTMRLLTLA LLFSCSVARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL 

        70         80         90        100        110        120 
NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG 

       130        140        150        160        170        180 
LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYSW NHIILLVSDD HEGRAAQKRL 

       190        200        210        220        230        240 
ETLLEERESK AEKVLQFDPG TKNVTALLME AKELEARVII LSASEDDAAT VYRAAAMLNM 

       250        260        270        280        290        300 
TGSGYVWLVG EREISGNALR YAPDGILGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN 

       310        320        330        340        350        360 
ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN YSIMNLQNRK 

       370        380        390        400        410        420 
LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI VTIHQEPFVY VKPTLSDGTC 

       430        440        450        460        470        480 
KEEFTVNGDP VKKVICTGPN DTSPGSPRHT VPQCCYGFCI DLLIKLARTM NFTYEVHLVA 

       490        500        510        520        530        540 
DGKFGTQERV NNSNKKEWNG MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI 

       550        560        570        580        590        600 
LVKKEIPRST LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA 

       610        620        630        640        650        660 
LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN LAAFLVLDRP 

       670        680        690        700        710        720 
EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS TMYRHMEKHN YESAAEAIQA 

       730        740        750        760        770        780 
VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH 

       790        800        810        820        830        840 
ENGFMEDLDK TWVRYQECDS RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH 

       850        860        870        880        890        900 
KDARRKQMQL AFAAVNVWRK NLQDRKSGRA EPDPKKKATF RAITSTLASS FKRRRSSKDT 

       910        920        930 
STGGGRGALQ NQKDTVLPRR AIEREEGQLQ LCSRHRES 

« Hide

Isoform 1 (Short) (NR1-1) [UniParc].

Checksum: 28C383037998DA20
Show »

FASTA88599,315
Isoform 2 (Medium) (NR1-2) [UniParc].

Checksum: E0C37E8C9F686155
Show »

FASTA901101,209
Isoform 4 [UniParc].

Checksum: F704AD9A244BD78E
Show »

FASTA922103,479
Isoform 5 [UniParc].

Checksum: C7F52E8535F521EE
Show »

FASTA959107,909
Isoform 6 [UniParc].

Checksum: 20DBA38A2B9E3ED0
Show »

FASTA943106,015
Isoform 7 [UniParc].

Checksum: B275FBD4126F4F15
Show »

FASTA906101,851

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of cDNAs encoding human hippocampus N-methyl-D-aspartate receptor subunits: evidence for alternative RNA splicing."
Foldes R.L., Rampersad V., Kamboj R.K.
Gene 131:293-298(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 11-938 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 300-938 (ISOFORM 2).
Tissue: Brain.
[2]"Molecular cloning and chromosomal localization of the key subunit of the human N-methyl-D-aspartate receptor."
Karp S.J., Masu M., Eki T., Ozawa K., Nakanishi S.
J. Biol. Chem. 268:3728-3733(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]"Molecular cloning, functional expression, and pharmacological characterization of an N-methyl-D-aspartate receptor subunit from human brain."
Planells-Cases R., Sun W., Ferrer-Montiel A.V., Montal M.
Proc. Natl. Acad. Sci. U.S.A. 90:5057-5061(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Cloning and structure of the gene encoding the human N-methyl-D-aspartate receptor (NMDAR1)."
Zimmer M., Fink T.M., Franke Y., Lichter P., Spiess J.
Gene 159:219-223(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Cloning and localization of exon 5-containing isoforms of the NMDAR1 subunit in human and rat brains."
Nash N.R., Heilman C.J., Rees H.D., Levey A.I.
J. Neurochem. 69:485-493(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7), VARIANTS MET-540 AND SER-682.
[6]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Cloning and sequence analysis of additional splice variants encoding human N-methyl-D-aspartate receptor (hNR1) subunits."
Foldes R.L., Rampersad V., Kamboj R.K.
Gene 147:303-304(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 332-922 (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] OF 86-259 (ISOFORM 5).
Tissue: Cerebellum and Hippocampus.
[8]"Inducible expression of neuronal glutamate receptor channels in the NT2 human cell line."
Younkin D.P., Tang C.-M., Hardy M., Reddy U.R., Shi Q.-Y., Pleasure S.J., Lee V.M.-Y., Pleasure D.
Proc. Natl. Acad. Sci. U.S.A. 90:2174-2178(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 364-464 (ISOFORMS 1/2/3).
[9]"Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain."
Tingley W.G., Roche K.W., Thompson A.K., Huganir R.L.
Nature 364:70-73(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PKC.
[10]"Appropriate NR1-NR1 disulfide-linked homodimer formation is requisite for efficient expression of functional, cell surface N-methyl-D-aspartate NR1/NR2 receptors."
Papadakis M., Hawkins L.M., Stephenson F.A.
J. Biol. Chem. 279:14703-14712(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERCHAIN DISULFIDE BOND.
[11]"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.
[12]"Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy."
Opella S.J., Marassi F.M., Gesell J.J., Valente A.P., Kim Y., Oblatt-Montal M., Montal M.
Nat. Struct. Biol. 6:374-379(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 599-621.
[13]"Excess of de novo deleterious mutations in genes associated with glutamatergic systems in nonsyndromic intellectual disability."
Hamdan F.F., Gauthier J., Araki Y., Lin D.T., Yoshizawa Y., Higashi K., Park A.R., Spiegelman D., Dobrzeniecka S., Piton A., Tomitori H., Daoud H., Massicotte C., Henrion E., Diallo O., Shekarabi M., Marineau C., Shevell M. expand/collapse author list , Maranda B., Mitchell G., Nadeau A., D'Anjou G., Vanasse M., Srour M., Lafreniere R.G., Drapeau P., Lacaille J.C., Kim E., Lee J.R., Igarashi K., Huganir R.L., Rouleau G.A., Michaud J.L.
Am. J. Hum. Genet. 88:306-316(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MRD8 SER-560 INS AND LYS-662, CHARACTERIZATION OF VARIANTS MRD8 SER-560 INS AND LYS-662.
+Additional computationally mapped references.

Web resources

Wikipedia

NMDA receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13266 mRNA. Translation: AAB59360.1.
L13267 mRNA. Translation: AAA36198.1.
L13268 mRNA. Translation: AAB59361.1.
D13515 mRNA. Translation: BAA02732.1.
L05666 mRNA. Translation: AAA21180.1.
AF015730 mRNA. Translation: AAB67723.1.
AF015731 mRNA. Translation: AAB67724.1.
Z32772 Genomic DNA. No translation available.
Z32773 Genomic DNA. No translation available.
Z32774 Genomic DNA. No translation available.
AL929554 Genomic DNA. Translation: CAH72874.2.
AL929554 Genomic DNA. Translation: CAH72875.2.
AL929554 Genomic DNA. Translation: CAH72876.2.
AL929554 Genomic DNA. Translation: CAH72879.2.
U08106 mRNA. Translation: AAA62111.1.
U08107 mRNA. Translation: AAA62112.1.
S57708 mRNA. Translation: AAB25917.1.
CCDSCCDS43910.1. [Q05586-2]
CCDS55354.1. [Q05586-6]
CCDS55355.1. [Q05586-7]
CCDS7031.1. [Q05586-1]
CCDS7032.1. [Q05586-3]
PIRA46612.
A47551.
RefSeqNP_000823.4. NM_000832.6. [Q05586-2]
NP_001172019.1. NM_001185090.1. [Q05586-6]
NP_001172020.1. NM_001185091.1. [Q05586-7]
NP_015566.1. NM_007327.3. [Q05586-1]
NP_067544.1. NM_021569.3. [Q05586-3]
XP_005266128.1. XM_005266071.1. [Q05586-4]
XP_005266130.1. XM_005266073.2. [Q05586-5]
UniGeneHs.558334.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HQWX-ray1.90B875-898[»]
2NR1NMR-A599-621[»]
3BYAX-ray1.85B875-898[»]
ProteinModelPortalQ05586.
SMRQ05586. Positions 24-838.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109159. 11 interactions.
IntActQ05586. 7 interactions.
MINTMINT-1900224.

Chemistry

BindingDBQ05586.
ChEMBLCHEMBL2015.
DrugBankDB00142. L-Glutamic Acid.
DB01173. Orphenadrine.
GuidetoPHARMACOLOGY455.

Protein family/group databases

TCDB1.A.10.1.6. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSiteQ05586.

Polymorphism databases

DMDM548377.

Proteomic databases

PaxDbQ05586.
PRIDEQ05586.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315048; ENSP00000316696; ENSG00000176884. [Q05586-4]
ENST00000371546; ENSP00000360601; ENSG00000176884. [Q05586-5]
ENST00000371550; ENSP00000360605; ENSG00000176884. [Q05586-3]
ENST00000371553; ENSP00000360608; ENSG00000176884. [Q05586-6]
ENST00000371559; ENSP00000360614; ENSG00000176884. [Q05586-2]
ENST00000371560; ENSP00000360615; ENSG00000176884. [Q05586-7]
ENST00000371561; ENSP00000360616; ENSG00000176884. [Q05586-1]
GeneID2902.
KEGGhsa:2902.
UCSCuc004clk.3. human. [Q05586-1]
uc004cll.3. human. [Q05586-3]
uc004clm.3. human. [Q05586-2]

Organism-specific databases

CTD2902.
GeneCardsGC09P140032.
HGNCHGNC:4584. GRIN1.
HPACAB006831.
MIM138249. gene.
614254. phenotype.
neXtProtNX_Q05586.
Orphanet178469. Autosomal dominant nonsyndromic intellectual disability.
PharmGKBPA28978.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282132.
HOVERGENHBG052638.
KOK05208.
OMAWNHVILL.
OrthoDBEOG79GT5V.
PhylomeDBQ05586.
TreeFamTF351405.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.
SignaLinkQ05586.

Gene expression databases

ArrayExpressQ05586.
BgeeQ05586.
CleanExHS_GRIN1.
GenevestigatorQ05586.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR018882. CaM-bd_C0_NMDA_rcpt_NR1.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
IPR001638. SBP_bac_3.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF10562. CaM_bdg_C0. 1 hit.
PF00060. Lig_chan. 1 hit.
PF00497. SBP_bac_3. 1 hit.
[Graphical view]
PRINTSPR00177. NMDARECEPTOR.
SMARTSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGRIN1. human.
EvolutionaryTraceQ05586.
GeneWikiGRIN1.
GenomeRNAi2902.
NextBio11487.
PMAP-CutDBQ5VSF3.
PROQ05586.
SOURCESearch...

Entry information

Entry nameNMDZ1_HUMAN
AccessionPrimary (citable) accession number: Q05586
Secondary accession number(s): A6NLK7 expand/collapse secondary AC list , A6NLR1, C9K0X1, P35437, Q12867, Q12868, Q5VSF3, Q5VSF4, Q5VSF5, Q5VSF6, Q5VSF7, Q5VSF8, Q9UPF8, Q9UPF9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM