Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutamate receptor ionotropic, NMDA 2B

Gene

GRIN2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi127ZincBy similarity1
Metal bindingi284ZincBy similarity1
Sitei615Functional determinant of NMDA receptorsBy similarity1

GO - Molecular functioni

  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • glycine binding Source: UniProtKB
  • NMDA glutamate receptor activity Source: ProtInc
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • chemical synaptic transmission Source: Reactome
  • ephrin receptor signaling pathway Source: Reactome
  • glutamate receptor signaling pathway Source: ProtInc
  • learning or memory Source: ProtInc
  • MAPK cascade Source: Reactome
  • response to ethanol Source: UniProtKB
  • transport Source: ProtInc
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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000150086-MONOMER.
ReactomeiR-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-HSA-442729. CREB phosphorylation through the activation of CaMKII.
R-HSA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6794361. Interactions of neurexins and neuroligins at synapses.
R-HSA-8849932. SALM protein interactions at the synapses.
SignaLinkiQ13224.
SIGNORiQ13224.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, NMDA 2B
Short name:
GluN2B
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-2
N-methyl D-aspartate receptor subtype 2B
Short name:
NMDAR2B
Short name:
NR2B
N-methyl-D-aspartate receptor subunit 3
Short name:
NR3
Short name:
hNR3
Gene namesi
Name:GRIN2B
Synonyms:NMDAR2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:4586. GRIN2B.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 557ExtracellularSequence analysisAdd BLAST531
Transmembranei558 – 578HelicalSequence analysisAdd BLAST21
Topological domaini579 – 634CytoplasmicSequence analysisAdd BLAST56
Transmembranei635 – 655HelicalSequence analysisAdd BLAST21
Topological domaini656 – 817ExtracellularSequence analysisAdd BLAST162
Transmembranei818 – 838HelicalSequence analysisAdd BLAST21
Topological domaini839 – 1484CytoplasmicSequence analysisAdd BLAST646

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cell surface Source: BHF-UCL
  • integral component of plasma membrane Source: ProtInc
  • intracellular Source: GOC
  • neuron projection Source: BHF-UCL
  • NMDA selective glutamate receptor complex Source: UniProtKB
  • plasma membrane Source: Reactome
  • postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal dominant 6 (MRD6)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
See also OMIM:613970
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076764456C → Y in MRD6. 1 Publication1
Natural variantiVAR_069384553P → L in MRD6. 1 PublicationCorresponds to variant rs397514556dbSNPEnsembl.1
Natural variantiVAR_065900682R → C in MRD6; analysis of agonist dose-response curves reveal no differences in the affinities of wild-type and mutant receptors for glutamate and glycine. 1 PublicationCorresponds to variant rs387906636dbSNPEnsembl.1
Epileptic encephalopathy, early infantile, 27 (EIEE27)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent.
See also OMIM:616139
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072663540R → H in EIEE27; gain of function mutation via an allosteric effect; the mutant channel is less sensitive to magnesium inhibition and has increased calcium permeability compared to wild-type. 1 PublicationCorresponds to variant rs672601378dbSNPEnsembl.1
Natural variantiVAR_072664615N → I in EIEE27; severe phenotype with early onset seizures; gain of function mutation; results in neuronal hyperexcitability; the mutant channel is not inhibited by magnesium and has increased calcium permeability compared to wild-type. 1 PublicationCorresponds to variant rs672601377dbSNPEnsembl.1
Natural variantiVAR_072665618V → G in EIEE27; severe phenotype with early onset seizures; gain of function mutation; results in neuronal hyperexcitability; the mutant channel is not inhibited by magnesium and has increased calcium permeability compared to wild-type. 1 PublicationCorresponds to variant rs672601376dbSNPEnsembl.1

A chromosomal aberrations involving GRIN2B has been found in patients with mental retardation. Translocations t(9;12)(p23;p13.1) and t(10;12)(q21.1;p13.1) with a common breakpoint in 12p13.1.

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

DisGeNETi2904.
MalaCardsiGRIN2B.
MIMi613970. phenotype.
616139. phenotype.
OpenTargetsiENSG00000273079.
Orphaneti178469. Autosomal dominant non-syndromic intellectual disability.
3451. West syndrome.
PharmGKBiPA28980.

Chemistry databases

ChEMBLiCHEMBL1904.
DrugBankiDB00659. Acamprosate.
DB06151. Acetylcysteine.
DB00289. Atomoxetine.
DB00949. Felbamate.
DB00996. Gabapentin.
DB00502. Haloperidol.
DB08954. Ifenprodil.
DB06738. Ketobemidone.
DB01043. Memantine.
DB04896. Milnacipran.
DB00312. Pentobarbital.
DB00454. Pethidine.
DB01174. Phenobarbital.
DB00418. Secobarbital.

Polymorphism and mutation databases

BioMutaiGRIN2B.
DMDMi14548162.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000001157727 – 1484Glutamate receptor ionotropic, NMDA 2BAdd BLAST1458

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi74N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi86 ↔ 321By similarity
Glycosylationi341N-linked (GlcNAc...)Sequence analysis1
Glycosylationi348N-linked (GlcNAc...)Sequence analysis1
Glycosylationi444N-linked (GlcNAc...)Sequence analysis1
Glycosylationi491N-linked (GlcNAc...)Sequence analysis1
Glycosylationi542N-linked (GlcNAc...)Sequence analysis1
Glycosylationi688N-linked (GlcNAc...)Sequence analysis1
Modified residuei882PhosphoserineBy similarity1
Modified residuei886PhosphoserineBy similarity1
Modified residuei917PhosphoserineBy similarity1
Modified residuei920PhosphoserineBy similarity1
Modified residuei962PhosphotyrosineBy similarity1
Modified residuei1039PhosphotyrosineBy similarity1
Modified residuei1058PhosphoserineBy similarity1
Modified residuei1061PhosphoserineBy similarity1
Modified residuei1064PhosphoserineBy similarity1
Modified residuei1109PhosphotyrosineBy similarity1
Modified residuei1133PhosphotyrosineBy similarity1
Modified residuei1143PhosphoserineBy similarity1
Modified residuei1155PhosphotyrosineBy similarity1
Modified residuei1255PhosphoserineBy similarity1
Modified residuei1259PhosphoserineBy similarity1
Modified residuei1303Phosphoserine; by DAPK1By similarity1
Modified residuei1474PhosphotyrosineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ13224.
PeptideAtlasiQ13224.
PRIDEiQ13224.

PTM databases

iPTMnetiQ13224.
PhosphoSitePlusiQ13224.

Expressioni

Tissue specificityi

Primarily found in the fronto-parieto-temporal cortex and hippocampus pyramidal cells, lower expression in the basal ganglia.1 Publication

Gene expression databases

BgeeiENSG00000273079.
CleanExiHS_GRIN2B.
ExpressionAtlasiQ13224. baseline and differential.
GenevisibleiQ13224. HS.

Organism-specific databases

HPAiHPA069762.

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 and GRIN3B. Found in a complex with GRIN1, GRIN3A and PPP2CB. Interacts with PDZ domains of PATJ and DLG4. Interacts with HIP1 and NETO1 (By similarity). Interacts with MAGI3. Interacts with DAPK1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CAMK2AQ9UQM73EBI-2256942,EBI-1383687
Dlg3Q629364EBI-2256942,EBI-349596From a different organism.
DLG4P783522EBI-2256942,EBI-80389
Dlg4P310162EBI-2256942,EBI-375655From a different organism.
PPP1CAP621392EBI-2256942,EBI-2008988From a different organism.

Protein-protein interaction databases

BioGridi109161. 25 interactors.
DIPiDIP-41002N.
IntActiQ13224. 13 interactors.
MINTiMINT-127466.
STRINGi9606.ENSP00000279593.

Chemistry databases

BindingDBiQ13224.

Structurei

Secondary structure

11484
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 44Combined sources11
Helixi47 – 50Combined sources4
Beta strandi62 – 73Combined sources12
Helixi78 – 91Combined sources14
Beta strandi94 – 100Combined sources7
Helixi107 – 119Combined sources13
Beta strandi123 – 127Combined sources5
Helixi128 – 131Combined sources4
Beta strandi143 – 147Combined sources5
Helixi150 – 164Combined sources15
Beta strandi168 – 173Combined sources6
Helixi179 – 191Combined sources13
Beta strandi193 – 195Combined sources3
Beta strandi198 – 204Combined sources7
Helixi215 – 221Combined sources7
Beta strandi226 – 232Combined sources7
Helixi234 – 246Combined sources13
Beta strandi255 – 258Combined sources4
Helixi260 – 263Combined sources4
Beta strandi278 – 282Combined sources5
Turni284 – 286Combined sources3
Helixi289 – 311Combined sources23
Beta strandi321 – 323Combined sources3
Helixi324 – 327Combined sources4
Helixi328 – 330Combined sources3
Helixi336 – 339Combined sources4
Beta strandi355 – 359Combined sources5
Beta strandi362 – 367Combined sources6
Beta strandi373 – 379Combined sources7
Beta strandi384 – 387Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S11model-A403-543[»]
B660-801[»]
1S2Smodel-A405-543[»]
B660-801[»]
2IPVmodel-X404-768[»]
5EWJX-ray2.77B/D31-394[»]
5EWLX-ray2.98B/D31-394[»]
5EWMX-ray2.76B/D31-394[»]
ProteinModelPortaliQ13224.
SMRiQ13224.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1292 – 1304Interaction with DAPK1By similarityAdd BLAST13

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1482 – 1484PDZ-bindingBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi984 – 989Poly-His6
Compositional biasi1361 – 1364Poly-His4

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
GeneTreeiENSGT00760000119186.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ13224.
KOiK05210.
OMAiCTNRSHL.
OrthoDBiEOG091G09KH.
PhylomeDBiQ13224.
TreeFamiTF314731.

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.

Q13224-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPRAECCSP KFWLVLAVLA VSGSRARSQK SPPSIGIAVI LVGTSDEVAI
60 70 80 90 100
KDAHEKDDFH HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVFA
110 120 130 140 150
DDTDQEAIAQ ILDFISAQTL TPILGIHGGS SMIMADKDES SMFFQFGPSI
160 170 180 190 200
EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ DFVNKIRSTI ENSFVGWELE
210 220 230 240 250
EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI FEVANSVGLT
260 270 280 290 300
GYGYTWIVPS LVAGDTDTVP AEFPTGLISV SYDEWDYGLP ARVRDGIAII
310 320 330 340 350
TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS
360 370 380 390 400
FSEDGYQMHP KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE
410 420 430 440 450
QEDDHLSIVT LEEAPFVIVE SVDPLSGTCM RNTVPCQKRI VTENKTDEEP
460 470 480 490 500
GYIKKCCKGF CIDILKKISK SVKFTYDLYL VTNGKHGKKI NGTWNGMIGE
510 520 530 540 550
VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR SNGTVSPSAF
560 570 580 590 600
LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF
610 620 630 640 650
TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL
660 670 680 690 700
AAFMIQEEYV DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA
710 720 730 740 750
EMHAYMGKFN QRGVDDALLS LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT
760 770 780 790 800
IGSGKVFAST GYGIAIQKDS GWKRQVDLAI LQLFGDGEME ELEALWLTGI
810 820 830 840 850
CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH LFYWQFRHCF
860 870 880 890 900
MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR
910 920 930 940 950
LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN
960 970 980 990 1000
NPPCEENLFS DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSASSI
1010 1020 1030 1040 1050
DGLYDCDNPP FTTQSRSISK KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS
1060 1070 1080 1090 1100
GHDDLIRSDV SDISTHTVTY GNIEGNAAKR RKQQYKDSLK KRPASAKSRR
1110 1120 1130 1140 1150
EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK ENSPHWEHVD
1160 1170 1180 1190 1200
LTDIYKERSD DFKRDSVSGG GPCTNRSHIK HGTGDKHGVV SGVPAPWEKN
1210 1220 1230 1240 1250
LTNVEWEDRS GGNFCRSCPS KLHNYSTTVT GQNSGRQACI RCEACKKAGN
1260 1270 1280 1290 1300
LYDISEDNSL QELDQPAAPV AVTSNASTTK YPQSPTNSKA QKKNRNKLRR
1310 1320 1330 1340 1350
QHSYDTFVDL QKEEAALAPR SVSLKDKGRF MDGSPYAHMF EMSAGESTFA
1360 1370 1380 1390 1400
NNKSSVPTAG HHHHNNPGGG YMLSKSLYPD RVTQNPFIPT FGDDQCLLHG
1410 1420 1430 1440 1450
SKSYFFRQPT VAGASKARPD FRALVTNKPV VSALHGAVPA RFQKDICIGN
1460 1470 1480
QSNPCVPNNK NPRAFNGSSN GHVYEKLSSI ESDV
Length:1,484
Mass (Da):166,367
Last modified:June 20, 2001 - v3
Checksum:i40AEB12BE6E50CEF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti434V → A in AAD00659 (Ref. 3) Curated1
Sequence conflicti745G → A in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti773K → N in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti773K → N in AAA74930 (PubMed:7959773).Curated1
Sequence conflicti796W → C in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti796W → C in AAA74930 (PubMed:7959773).Curated1
Sequence conflicti888T → P in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti888T → P in AAA74930 (PubMed:7959773).Curated1
Sequence conflicti902L → V in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti902L → V in AAA74930 (PubMed:7959773).Curated1
Sequence conflicti920 – 921SA → RP in AAB60368 (PubMed:7999784).Curated2
Sequence conflicti958L → S in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti958L → S in AAA74930 (PubMed:7959773).Curated1
Sequence conflicti980 – 982VYQ → DHY in AAA69920 (PubMed:7959773).Curated3
Sequence conflicti1056I → M in AAA69920 (PubMed:7959773).Curated1
Sequence conflicti1167V → I in AAB49993 (PubMed:8768735).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_011317407S → N.1 Publication1
Natural variantiVAR_076764456C → Y in MRD6. 1 Publication1
Natural variantiVAR_072663540R → H in EIEE27; gain of function mutation via an allosteric effect; the mutant channel is less sensitive to magnesium inhibition and has increased calcium permeability compared to wild-type. 1 PublicationCorresponds to variant rs672601378dbSNPEnsembl.1
Natural variantiVAR_069384553P → L in MRD6. 1 PublicationCorresponds to variant rs397514556dbSNPEnsembl.1
Natural variantiVAR_072664615N → I in EIEE27; severe phenotype with early onset seizures; gain of function mutation; results in neuronal hyperexcitability; the mutant channel is not inhibited by magnesium and has increased calcium permeability compared to wild-type. 1 PublicationCorresponds to variant rs672601377dbSNPEnsembl.1
Natural variantiVAR_072665618V → G in EIEE27; severe phenotype with early onset seizures; gain of function mutation; results in neuronal hyperexcitability; the mutant channel is not inhibited by magnesium and has increased calcium permeability compared to wild-type. 1 PublicationCorresponds to variant rs672601376dbSNPEnsembl.1
Natural variantiVAR_065900682R → C in MRD6; analysis of agonist dose-response curves reveal no differences in the affinities of wild-type and mutant receptors for glutamate and glycine. 1 PublicationCorresponds to variant rs387906636dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90278 mRNA. Translation: AAB49993.1.
U88963 mRNA. Translation: AAD00659.1.
U11287 mRNA. Translation: AAB60368.1.
BC113618 mRNA. Translation: AAI13619.1.
BC113620 mRNA. Translation: AAI13621.1.
U28758 mRNA. Translation: AAA74930.1.
U28861 mRNA. Translation: AAA69919.1.
U28862 mRNA. Translation: AAA69920.1.
CCDSiCCDS8662.1.
PIRiI39066.
S52086.
RefSeqiNP_000825.2. NM_000834.3.
XP_011518930.1. XM_011520628.2.
XP_011518931.1. XM_011520629.2.
XP_016874708.1. XM_017019219.1.
UniGeneiHs.504844.
Hs.632856.
Hs.654430.

Genome annotation databases

EnsembliENST00000609686; ENSP00000477455; ENSG00000273079.
GeneIDi2904.
KEGGihsa:2904.
UCSCiuc001rbt.3. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90278 mRNA. Translation: AAB49993.1.
U88963 mRNA. Translation: AAD00659.1.
U11287 mRNA. Translation: AAB60368.1.
BC113618 mRNA. Translation: AAI13619.1.
BC113620 mRNA. Translation: AAI13621.1.
U28758 mRNA. Translation: AAA74930.1.
U28861 mRNA. Translation: AAA69919.1.
U28862 mRNA. Translation: AAA69920.1.
CCDSiCCDS8662.1.
PIRiI39066.
S52086.
RefSeqiNP_000825.2. NM_000834.3.
XP_011518930.1. XM_011520628.2.
XP_011518931.1. XM_011520629.2.
XP_016874708.1. XM_017019219.1.
UniGeneiHs.504844.
Hs.632856.
Hs.654430.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S11model-A403-543[»]
B660-801[»]
1S2Smodel-A405-543[»]
B660-801[»]
2IPVmodel-X404-768[»]
5EWJX-ray2.77B/D31-394[»]
5EWLX-ray2.98B/D31-394[»]
5EWMX-ray2.76B/D31-394[»]
ProteinModelPortaliQ13224.
SMRiQ13224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109161. 25 interactors.
DIPiDIP-41002N.
IntActiQ13224. 13 interactors.
MINTiMINT-127466.
STRINGi9606.ENSP00000279593.

Chemistry databases

BindingDBiQ13224.
ChEMBLiCHEMBL1904.
DrugBankiDB00659. Acamprosate.
DB06151. Acetylcysteine.
DB00289. Atomoxetine.
DB00949. Felbamate.
DB00996. Gabapentin.
DB00502. Haloperidol.
DB08954. Ifenprodil.
DB06738. Ketobemidone.
DB01043. Memantine.
DB04896. Milnacipran.
DB00312. Pentobarbital.
DB00454. Pethidine.
DB01174. Phenobarbital.
DB00418. Secobarbital.

PTM databases

iPTMnetiQ13224.
PhosphoSitePlusiQ13224.

Polymorphism and mutation databases

BioMutaiGRIN2B.
DMDMi14548162.

Proteomic databases

PaxDbiQ13224.
PeptideAtlasiQ13224.
PRIDEiQ13224.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000609686; ENSP00000477455; ENSG00000273079.
GeneIDi2904.
KEGGihsa:2904.
UCSCiuc001rbt.3. human.

Organism-specific databases

CTDi2904.
DisGeNETi2904.
GeneCardsiGRIN2B.
H-InvDBHIX0036873.
HGNCiHGNC:4586. GRIN2B.
HPAiHPA069762.
MalaCardsiGRIN2B.
MIMi138252. gene.
613970. phenotype.
616139. phenotype.
neXtProtiNX_Q13224.
OpenTargetsiENSG00000273079.
Orphaneti178469. Autosomal dominant non-syndromic intellectual disability.
3451. West syndrome.
PharmGKBiPA28980.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
GeneTreeiENSGT00760000119186.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ13224.
KOiK05210.
OMAiCTNRSHL.
OrthoDBiEOG091G09KH.
PhylomeDBiQ13224.
TreeFamiTF314731.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000150086-MONOMER.
ReactomeiR-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-HSA-442729. CREB phosphorylation through the activation of CaMKII.
R-HSA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6794361. Interactions of neurexins and neuroligins at synapses.
R-HSA-8849932. SALM protein interactions at the synapses.
SignaLinkiQ13224.
SIGNORiQ13224.

Miscellaneous databases

GeneWikiiGRIN2B.
GenomeRNAii2904.
PROiQ13224.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000273079.
CleanExiHS_GRIN2B.
ExpressionAtlasiQ13224. baseline and differential.
GenevisibleiQ13224. HS.

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...

Entry informationi

Entry nameiNMDE2_HUMAN
AccessioniPrimary (citable) accession number: Q13224
Secondary accession number(s): Q12919
, Q13220, Q13225, Q14CU4, Q9UM56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 20, 2001
Last modified: November 2, 2016
This is version 173 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.