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Protein

Glutamate receptor ionotropic, NMDA 2B

Gene

Grin2b

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 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 bindingi127Zinc1
Metal bindingi284Zinc1
Sitei615Functional determinant of NMDA receptorsBy similarity1

GO - Molecular functioni

  • beta-catenin binding Source: RGD
  • cell adhesion molecule binding Source: RGD
  • D2 dopamine receptor binding Source: RGD
  • drug binding Source: RGD
  • extracellular-glutamate-gated ion channel activity Source: RGD
  • interleukin-1 receptor binding Source: RGD
  • ionotropic glutamate receptor activity Source: RGD
  • ionotropic glutamate receptor binding Source: RGD
  • neurotransmitter binding Source: RGD
  • NMDA glutamate receptor activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • receptor binding Source: RGD
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • action potential Source: RGD
  • associative learning Source: RGD
  • cellular response to amino acid stimulus Source: RGD
  • cellular response to dsRNA Source: RGD
  • cellular response to growth factor stimulus Source: RGD
  • cellular response to lipid Source: RGD
  • cellular response to magnesium starvation Source: RGD
  • cellular response to manganese ion Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • cerebral cortex development Source: RGD
  • hippocampus development Source: RGD
  • ionotropic glutamate receptor signaling pathway Source: RGD
  • learning or memory Source: RGD
  • long-term memory Source: RGD
  • memory Source: UniProtKB
  • multicellular organismal response to stress Source: RGD
  • positive regulation of cell death Source: RGD
  • positive regulation of glutamate secretion Source: UniProtKB
  • positive regulation of synaptic transmission Source: RGD
  • receptor clustering Source: RGD
  • regulation of long-term neuronal synaptic plasticity Source: RGD
  • regulation of MAPK cascade Source: UniProtKB
  • response to amine Source: RGD
  • response to amphetamine Source: RGD
  • response to calcium ion Source: RGD
  • response to carbohydrate Source: RGD
  • response to cocaine Source: RGD
  • response to cytokine Source: RGD
  • response to electrical stimulus Source: RGD
  • response to ethanol Source: RGD
  • response to fungicide Source: RGD
  • response to growth hormone Source: RGD
  • response to magnesium ion Source: RGD
  • response to manganese ion Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to methylmercury Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to other organism Source: RGD
  • response to toxic substance Source: RGD
  • rhythmic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-6794361. Interactions of neurexins and neuroligins at synapses.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, NMDA 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 namesi
Name:Grin2b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2738. 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 – 1482CytoplasmicSequence analysisAdd BLAST644

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi60H → A: Normal zinc binding. 1 Publication1
Mutagenesisi127H → A: Reduced zinc binding. 1
Mutagenesisi283D → A: Slightly reduced zinc binding. 1
Mutagenesisi284E → A: Reduced zinc binding. 1
Mutagenesisi311H → A: Normal zinc binding. 1 Publication1
Mutagenesisi359H → A: Normal zinc binding. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL311.
GuidetoPHARMACOLOGYi457.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000001157927 – 1482Glutamate receptor ionotropic, NMDA 2BAdd BLAST1456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi74N-linked (GlcNAc...)1 Publication1
Disulfide bondi86 ↔ 3211 Publication
Glycosylationi341N-linked (GlcNAc...)1 Publication1
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 residuei882PhosphoserineCombined sources1
Modified residuei886PhosphoserineCombined sources1
Modified residuei917PhosphoserineCombined sources1
Modified residuei920PhosphoserineCombined sources1
Modified residuei962PhosphotyrosineBy similarity1
Modified residuei1039PhosphotyrosineCombined sources1
Modified residuei1058PhosphoserineBy similarity1
Modified residuei1061PhosphoserineBy similarity1
Modified residuei1064PhosphoserineBy similarity1
Modified residuei1109PhosphotyrosineBy similarity1
Modified residuei1133PhosphotyrosineBy similarity1
Modified residuei1143PhosphoserineBy similarity1
Modified residuei1155PhosphotyrosineBy similarity1
Modified residuei1255PhosphoserineCombined sources1
Modified residuei1259PhosphoserineCombined sources1
Modified residuei1303PhosphoserineCombined sources1
Modified residuei1472PhosphotyrosineBy 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

PaxDbiQ00960.
PRIDEiQ00960.

PTM databases

iPTMnetiQ00960.
PhosphoSitePlusiQ00960.
SwissPalmiQ00960.
UniCarbKBiQ00960.

Interactioni

Subunit structurei

Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A or GRIN3B). Found in a complex with GRIN1, GRIN3A and PPP2CB. Found in a complex with GRIN1 and GRIN3B. Interacts with MAGI3. Interacts with HIP1 and Neto1 (By similarity). Interacts with PDZ domains of PATJ and DLG4. Interacts with DAPK1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Camk2aP112752EBI-396905,EBI-2640645
Camk2aP117983EBI-396905,EBI-400384From a different organism.
Dlg3Q629366EBI-396905,EBI-349596
Dlg4P310168EBI-396905,EBI-375655
InadlQ63ZW74EBI-396905,EBI-8366894From a different organism.
Lrfn2Q460M52EBI-396905,EBI-877185

GO - Molecular functioni

  • beta-catenin binding Source: RGD
  • cell adhesion molecule binding Source: RGD
  • D2 dopamine receptor binding Source: RGD
  • interleukin-1 receptor binding Source: RGD
  • ionotropic glutamate receptor binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • receptor binding Source: RGD

Protein-protein interaction databases

BioGridi246575. 12 interactors.
DIPiDIP-33702N.
IntActiQ00960. 16 interactors.
MINTiMINT-104014.
STRINGi10116.ENSRNOP00000011697.

Chemistry databases

BindingDBiQ00960.

Structurei

Secondary structure

11482
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 44Combined sources11
Helixi47 – 50Combined sources4
Helixi53 – 55Combined sources3
Beta strandi64 – 73Combined sources10
Helixi78 – 91Combined sources14
Beta strandi94 – 103Combined sources10
Helixi107 – 119Combined sources13
Beta strandi123 – 127Combined sources5
Helixi128 – 131Combined sources4
Beta strandi143 – 147Combined sources5
Helixi150 – 163Combined sources14
Beta strandi168 – 175Combined sources8
Helixi179 – 191Combined sources13
Beta strandi198 – 205Combined sources8
Beta strandi211 – 213Combined sources3
Helixi215 – 220Combined sources6
Beta strandi226 – 232Combined sources7
Helixi234 – 245Combined sources12
Turni246 – 248Combined sources3
Beta strandi251 – 253Combined sources3
Beta strandi255 – 258Combined sources4
Helixi260 – 263Combined sources4
Beta strandi275 – 281Combined sources7
Turni284 – 286Combined sources3
Helixi289 – 308Combined sources20
Turni309 – 311Combined sources3
Turni322 – 326Combined sources5
Helixi327 – 330Combined sources4
Helixi336 – 339Combined sources4
Beta strandi355 – 359Combined sources5
Beta strandi362 – 367Combined sources6
Beta strandi369 – 371Combined sources3
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
3JPWX-ray2.80A32-394[»]
3JPYX-ray3.21A32-394[»]
3QELX-ray2.60B/D31-394[»]
3QEMX-ray3.00B/D31-394[»]
4PE5X-ray3.96B/D27-852[»]
5B3JX-ray2.90C/D31-394[»]
5FXGelectron microscopy6.80B/D27-852[»]
5FXHelectron microscopy6.10B/D27-852[»]
5FXIelectron microscopy6.40B/D27-852[»]
5FXJelectron microscopy6.50B/D27-852[»]
5FXKelectron microscopy6.40B/D27-852[»]
ProteinModelPortaliQ00960.
SMRiQ00960.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00960.

Family & Domainsi

Region

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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1480 – 1482PDZ-binding3

Compositional bias

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

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ00960.
KOiK05210.
PhylomeDBiQ00960.

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.

Q00960-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPSAECCSP KFWLVLAVLA VSGSKARSQK 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 SEFPTGLISV 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 ISENKTDEEP
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 PHSIGSTSSI
1010 1020 1030 1040 1050
DGLYDCDNPP FTTQPRSISK 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 GPCTNRSHLK HGTGEKHGVV GGVPAPWEKN
1210 1220 1230 1240 1250
LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN
1260 1270 1280 1290 1300
LYDISEDNSL QELDQPAAPV AVTSNASSTK YPQSPTNSKA QKKNRNKLRR
1310 1320 1330 1340 1350
QHSYDTFVDL QKEEAALAPR SVSLKDKGRF MDGSPYAHMF EMPAGESSFA
1360 1370 1380 1390 1400
NKSSVPTAGH HHNNPGSGYM LSKSLYPDRV TQNPFIPTFG DDQCLLHGSK
1410 1420 1430 1440 1450
SYFFRQPTVA GASKTRPDFR ALVTNKPVVV TLHGAVPGRF QKDICIGNQS
1460 1470 1480
NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV
Length:1,482
Mass (Da):166,071
Last modified:June 1, 1994 - v1
Checksum:iAEF8B9DF3C1B0D5D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1256E → K in AAA50554 (PubMed:7524561).Curated1
Sequence conflicti1430 – 1431VT → SA in AAA50554 (PubMed:7524561).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91562 mRNA. Translation: AAA41714.1.
U11419 mRNA. Translation: AAA50554.1.
PIRiB43274.
RefSeqiNP_036706.1. NM_012574.1.
UniGeneiRn.9711.

Genome annotation databases

GeneIDi24410.
KEGGirno:24410.
UCSCiRGD:2738. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91562 mRNA. Translation: AAA41714.1.
U11419 mRNA. Translation: AAA50554.1.
PIRiB43274.
RefSeqiNP_036706.1. NM_012574.1.
UniGeneiRn.9711.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JPWX-ray2.80A32-394[»]
3JPYX-ray3.21A32-394[»]
3QELX-ray2.60B/D31-394[»]
3QEMX-ray3.00B/D31-394[»]
4PE5X-ray3.96B/D27-852[»]
5B3JX-ray2.90C/D31-394[»]
5FXGelectron microscopy6.80B/D27-852[»]
5FXHelectron microscopy6.10B/D27-852[»]
5FXIelectron microscopy6.40B/D27-852[»]
5FXJelectron microscopy6.50B/D27-852[»]
5FXKelectron microscopy6.40B/D27-852[»]
ProteinModelPortaliQ00960.
SMRiQ00960.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246575. 12 interactors.
DIPiDIP-33702N.
IntActiQ00960. 16 interactors.
MINTiMINT-104014.
STRINGi10116.ENSRNOP00000011697.

Chemistry databases

BindingDBiQ00960.
ChEMBLiCHEMBL311.
GuidetoPHARMACOLOGYi457.

Protein family/group databases

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

PTM databases

iPTMnetiQ00960.
PhosphoSitePlusiQ00960.
SwissPalmiQ00960.
UniCarbKBiQ00960.

Proteomic databases

PaxDbiQ00960.
PRIDEiQ00960.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24410.
KEGGirno:24410.
UCSCiRGD:2738. rat.

Organism-specific databases

CTDi2904.
RGDi2738. Grin2b.

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ00960.
KOiK05210.
PhylomeDBiQ00960.

Enzyme and pathway databases

ReactomeiR-RNO-6794361. Interactions of neurexins and neuroligins at synapses.

Miscellaneous databases

EvolutionaryTraceiQ00960.
PROiQ00960.

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_RAT
AccessioniPrimary (citable) accession number: Q00960
Secondary accession number(s): Q62684
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 161 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

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.