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Q00960 (NMDE2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Grin2b
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length1482 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. 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.

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). 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. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein.

Post-translational modification

Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity By similarity.

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR2B/GRIN2B subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCalcium
Magnesium
Metal-binding
Zinc
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processassociative learning

Inferred from mutant phenotype PubMed 17328778. Source: RGD

cellular response to amino acid stimulus

Inferred from expression pattern PubMed 20336776PubMed 20526740. Source: RGD

cellular response to dsRNA

Inferred from expression pattern PubMed 19958814. Source: RGD

cellular response to growth factor stimulus

Inferred from expression pattern PubMed 19958814. Source: RGD

cellular response to lipid

Inferred from expression pattern PubMed 19819306. Source: RGD

cellular response to magnesium starvation

Inferred from expression pattern PubMed 17428633. Source: RGD

cellular response to manganese ion

Inferred from expression pattern PubMed 19643132. Source: RGD

cerebral cortex development

Inferred from expression pattern PubMed 19409459. Source: RGD

hippocampus development

Inferred from expression pattern PubMed 19535712. Source: RGD

long-term memory

Inferred from expression pattern PubMed 20581725. Source: RGD

multicellular organismal response to stress

Inferred from expression pattern PubMed 20309729. Source: RGD

positive regulation of cell death

Inferred from direct assay PubMed 20168047. Source: RGD

positive regulation of glutamate secretion

Inferred from direct assay PubMed 16407536. Source: UniProtKB

positive regulation of synaptic transmission

Inferred from mutant phenotype PubMed 19208366. Source: RGD

receptor clustering

Inferred from direct assay PubMed 20008487. Source: RGD

regulation of MAPK cascade

Inferred from mutant phenotype PubMed 14622581. Source: UniProtKB

regulation of action potential

Inferred from mutant phenotype PubMed 16904707PubMed 17655746. Source: RGD

regulation of long-term neuronal synaptic plasticity

Inferred from mutant phenotype PubMed 16904707PubMed 17655746. Source: RGD

response to amphetamine

Inferred from expression pattern PubMed 20422365. Source: RGD

response to calcium ion

Inferred from expression pattern PubMed 19761817. Source: RGD

response to carbohydrate stimulus

Inferred from expression pattern PubMed 19695778. Source: RGD

response to cocaine

Inferred from expression pattern PubMed 19322657. Source: RGD

response to cytokine stimulus

Inferred from expression pattern PubMed 20005040. Source: RGD

response to electrical stimulus

Inferred from expression pattern PubMed 20514696. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 19673743. Source: RGD

response to fungicide

Inferred from expression pattern PubMed 19591855. Source: RGD

response to growth hormone stimulus

Inferred from expression pattern PubMed 20237303. Source: RGD

response to magnesium ion

Inferred from expression pattern PubMed 20152124. Source: RGD

response to mechanical stimulus

Inferred from expression pattern PubMed 19778590. Source: RGD

response to methylmercury

Inferred from expression pattern PubMed 19409459. Source: RGD

response to other organism

Inferred from expression pattern PubMed 19563853. Source: RGD

rhythmic process

Inferred from direct assay PubMed 16477151. Source: RGD

   Cellular_componentN-methyl-D-aspartate selective glutamate receptor complex

Inferred from direct assay PubMed 8702950. Source: UniProtKB

Z disc

Inferred from direct assay PubMed 15010472. Source: RGD

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

outer membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

postsynaptic density

Inferred from direct assay PubMed 17145509PubMed 17207780. Source: RGD

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

presynaptic membrane

Inferred from direct assay PubMed 16157280. Source: UniProtKB

synaptic cleft

Inferred from direct assay PubMed 17207780. Source: RGD

terminal bouton

Inferred from direct assay PubMed 19666514. Source: RGD

   Molecular_functionN-methyl-D-aspartate selective glutamate receptor activity

Inferred from direct assay Ref.1PubMed 16477151. Source: RGD

drug binding

Inferred from physical interaction PubMed 20082612. Source: RGD

extracellular-glutamate-gated ion channel activity

Inferred from direct assay Ref.1. Source: RGD

neurotransmitter binding

Inferred from direct assay PubMed 16477151. Source: RGD

protein heterodimerization activity

Inferred from direct assay Ref.1PubMed 21544205. Source: RGD

zinc ion binding

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dlg4P310165EBI-396905,EBI-375655
Lrfn2Q460M52EBI-396905,EBI-877185

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 14821456Glutamate receptor ionotropic, NMDA 2B
PRO_0000011579

Regions

Topological domain27 – 557531Extracellular Potential
Transmembrane558 – 57821Helical; Potential
Topological domain579 – 63456Cytoplasmic Potential
Transmembrane635 – 65521Helical; Potential
Topological domain656 – 817162Extracellular Potential
Transmembrane818 – 83821Helical; Potential
Topological domain839 – 1482644Cytoplasmic Potential
Region1292 – 130413Interaction with DAPK1 By similarity
Motif1480 – 14823PDZ-binding
Compositional bias984 – 9896Poly-His

Sites

Metal binding1271Zinc
Metal binding2841Zinc
Site6151Functional determinant of NMDA receptors By similarity

Amino acid modifications

Modified residue9171Phosphoserine By similarity
Modified residue9301Phosphoserine By similarity
Modified residue9321Phosphotyrosine By similarity
Modified residue9491Phosphotyrosine By similarity
Modified residue9621Phosphotyrosine By similarity
Modified residue10391Phosphotyrosine By similarity
Modified residue10491Phosphotyrosine By similarity
Modified residue10611Phosphoserine By similarity
Modified residue10651Phosphothreonine By similarity
Modified residue10701Phosphotyrosine By similarity
Modified residue11091Phosphotyrosine By similarity
Modified residue11551Phosphotyrosine By similarity
Modified residue11661Phosphoserine By similarity
Modified residue12521Phosphotyrosine By similarity
Modified residue13031Phosphoserine; by DAPK1 By similarity
Modified residue14721Phosphotyrosine By similarity
Glycosylation741N-linked (GlcNAc...) Ref.9
Glycosylation3411N-linked (GlcNAc...) Ref.9
Glycosylation3481N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential
Glycosylation5421N-linked (GlcNAc...) Potential
Glycosylation6881N-linked (GlcNAc...) Potential
Disulfide bond86 ↔ 321 Ref.9

Experimental info

Mutagenesis601H → A: Normal zinc binding. Ref.9
Mutagenesis1271H → A: Reduced zinc binding.
Mutagenesis2831D → A: Slightly reduced zinc binding.
Mutagenesis2841E → A: Reduced zinc binding.
Mutagenesis3111H → A: Normal zinc binding. Ref.9
Mutagenesis3591H → A: Normal zinc binding. Ref.9
Sequence conflict12561E → K in AAA50554. Ref.2
Sequence conflict1430 – 14312VT → SA in AAA50554. Ref.2

Secondary structure

1 ................................................................. 1482
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00960 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: AEF8B9DF3C1B0D5D

FASTA1,482166,071
        10         20         30         40         50         60 
MKPSAECCSP KFWLVLAVLA VSGSKARSQK SPPSIGIAVI LVGTSDEVAI KDAHEKDDFH 

        70         80         90        100        110        120 
HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVFA DDTDQEAIAQ ILDFISAQTL 

       130        140        150        160        170        180 
TPILGIHGGS SMIMADKDES SMFFQFGPSI EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ 

       190        200        210        220        230        240 
DFVNKIRSTI ENSFVGWELE EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI 

       250        260        270        280        290        300 
FEVANSVGLT GYGYTWIVPS LVAGDTDTVP SEFPTGLISV SYDEWDYGLP ARVRDGIAII 

       310        320        330        340        350        360 
TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS FSEDGYQMHP 

       370        380        390        400        410        420 
KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE QEDDHLSIVT LEEAPFVIVE 

       430        440        450        460        470        480 
SVDPLSGTCM RNTVPCQKRI ISENKTDEEP GYIKKCCKGF CIDILKKISK SVKFTYDLYL 

       490        500        510        520        530        540 
VTNGKHGKKI NGTWNGMIGE VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR 

       550        560        570        580        590        600 
SNGTVSPSAF LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF 

       610        620        630        640        650        660 
TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL AAFMIQEEYV 

       670        680        690        700        710        720 
DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA EMHAYMGKFN QRGVDDALLS 

       730        740        750        760        770        780 
LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT IGSGKVFAST GYGIAIQKDS GWKRQVDLAI 

       790        800        810        820        830        840 
LQLFGDGEME ELEALWLTGI CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH 

       850        860        870        880        890        900 
LFYWQFRHCF MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR 

       910        920        930        940        950        960 
LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN NPPCEENLFS 

       970        980        990       1000       1010       1020 
DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSTSSI DGLYDCDNPP FTTQPRSISK 

      1030       1040       1050       1060       1070       1080 
KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS GHDDLIRSDV SDISTHTVTY GNIEGNAAKR 

      1090       1100       1110       1120       1130       1140 
RKQQYKDSLK KRPASAKSRR EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK 

      1150       1160       1170       1180       1190       1200 
ENSPHWEHVD LTDIYKERSD DFKRDSVSGG GPCTNRSHLK HGTGEKHGVV GGVPAPWEKN 

      1210       1220       1230       1240       1250       1260 
LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN LYDISEDNSL 

      1270       1280       1290       1300       1310       1320 
QELDQPAAPV AVTSNASSTK YPQSPTNSKA QKKNRNKLRR QHSYDTFVDL QKEEAALAPR 

      1330       1340       1350       1360       1370       1380 
SVSLKDKGRF MDGSPYAHMF EMPAGESSFA NKSSVPTAGH HHNNPGSGYM LSKSLYPDRV 

      1390       1400       1410       1420       1430       1440 
TQNPFIPTFG DDQCLLHGSK SYFFRQPTVA GASKTRPDFR ALVTNKPVVV TLHGAVPGRF 

      1450       1460       1470       1480 
QKDICIGNQS NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M91562 mRNA. Translation: AAA41714.1.
U11419 mRNA. Translation: AAA50554.1.
IPIIPI00326061.
PIRB43274.
RefSeqNP_036706.1. NM_012574.1.
UniGeneRn.9711.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3JPWX-ray2.80A32-394[»]
3JPYX-ray3.21A32-394[»]
3QELX-ray2.60B/D31-394[»]
3QEMX-ray3.00B/D31-394[»]
ProteinModelPortalQ00960.
SMRQ00960. Positions 404-802.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-33702N.
IntActQ00960. 2 interactions.
MINTMINT-104014.
STRING10116.ENSRNOP00000011697.

Protein family/group databases

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

PTM databases

PhosphoSiteQ00960.

Proteomic databases

PaxDbQ00960.
PRIDEQ00960.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24410.
KEGGrno:24410.
UCSCRGD:2738. rat.

Organism-specific databases

CTD2904.
RGD2738. Grin2b.

Phylogenomic databases

eggNOGNOG282132.
HOGENOMHOG000113802.
HOVERGENHBG052635.
InParanoidQ00960.
KOK05210.
OrthoDBEOG4Z8XVM.

Gene expression databases

GenevestigatorQ00960.
GermOnlineENSRNOG00000008766. Rattus norvegicus.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR018884. NMDAR2_C.
IPR001638. SBP_bac_3.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10565. NMDAR2_C. 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]
ProtoNetSearch...

Other

BindingDBQ00960.
ChEMBLCHEMBL311.
EvolutionaryTraceQ00960.
NextBio603231.

Entry information

Entry nameNMDE2_RAT
AccessionPrimary (citable) accession number: Q00960
Secondary accession number(s): Q62684
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 3, 2013
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents