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Protein

Glutamate receptor ionotropic, NMDA 2B

Gene

Grin2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg2+ (PubMed:1377365, PubMed:26912815). Sensitivity to glutamate and channel kinetics depend on the subunit composition (PubMed:1377365). 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 (PubMed:20141836). Contributes to neural pattern formation in the developing brain (PubMed:8789948). Plays a role in long-term depression (LTD) of hippocampus membrane currents and in synaptic plasticity (PubMed:8789948).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi127ZincBy similarity1
Metal bindingi284ZincBy similarity1
Binding sitei514GlutamateBy similarity1
Binding sitei519GlutamateBy similarity1
Sitei615Functional determinant of NMDA receptorsBy similarity1
Binding sitei732GlutamateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport
LigandCalcium, Magnesium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, NMDA 2B
Short name:
GluN2B
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-21 Publication
N-methyl D-aspartate receptor subtype 2B
Short name:
NMDAR2B
Short name:
NR2B
Gene namesi
Name:Grin2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:95821 Grin2b

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 557ExtracellularBy similarityAdd BLAST531
Transmembranei558 – 576HelicalBy similarityAdd BLAST19
Topological domaini577 – 603CytoplasmicBy similarityAdd BLAST27
Intramembranei604 – 623Discontinuously helicalBy similarityAdd BLAST20
Topological domaini624 – 630CytoplasmicBy similarity7
Transmembranei631 – 646HelicalBy similarityAdd BLAST16
Topological domaini647 – 817ExtracellularBy similarityAdd BLAST171
Transmembranei818 – 837HelicalBy similarityAdd BLAST20
Topological domaini838 – 1482CytoplasmicBy similarityAdd BLAST645

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

Mutant pups are born at the expected Mendelian rate and appear grossly normal, but lack suckling behavior. As a consequence, all die shortly after birth, except when they are fed manually via a soft tube that delivers milk directly into the stomach. While mutant neonate brain structures are grossly normal, the mutant brain stem trigeminal complex lacks the neural repeating units called barrelettes that correspond to whisker-associated nerve fibers. Primary afferent nerve fibers from whiskers fail to show normal clustering in the region where barrelette structures form in wild-type. In contrast, nasolabial motor neurons appear normal. Contrary to wild-type neonates, brain slices from the mutant neonate hippocampus CA1 region lack NMDA receptor-type ion channel activity. Contrary to wild-type pups, prolonged low frequency stimulation of afferent fibers does not induce long-term depression (LTD) in the hippocampus.1 Publication

Chemistry databases

ChEMBLiCHEMBL3442

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000001157827 – 1482Glutamate receptor ionotropic, NMDA 2BAdd BLAST1456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi74N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi86 ↔ 321By similarity
Glycosylationi341N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi348N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi429 ↔ 456By similarity
Disulfide bondi436 ↔ 457By similarity
Glycosylationi444N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi491N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi542N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi688N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi746 ↔ 801By similarity
Modified residuei882PhosphoserineCombined sources1
Modified residuei886PhosphoserineBy similarity1
Modified residuei917PhosphoserineCombined sources1
Modified residuei920PhosphoserineCombined sources1
Modified residuei962PhosphotyrosineCombined sources1
Modified residuei1039PhosphotyrosineCombined sources1
Modified residuei1058PhosphoserineCombined sources1
Modified residuei1061PhosphoserineCombined sources1
Modified residuei1064PhosphoserineCombined sources1
Modified residuei1109PhosphotyrosineCombined sources1
Modified residuei1133PhosphotyrosineCombined sources1
Modified residuei1143PhosphoserineCombined sources1
Modified residuei1155PhosphotyrosineCombined sources1
Modified residuei1255PhosphoserineCombined sources1
Modified residuei1259PhosphoserineCombined sources1
Modified residuei1303Phosphoserine; by DAPK1Combined sources1 Publication1
Modified residuei1472Phosphotyrosine1 Publication1

Post-translational modificationi

Phosphorylated on tyrosine residues (PubMed:12451687). Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity (PubMed:20141836).2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ01097
PaxDbiQ01097
PRIDEiQ01097

PTM databases

iPTMnetiQ01097
PhosphoSitePlusiQ01097
SwissPalmiQ01097

Expressioni

Tissue specificityi

Detected in brain (at protein level) (PubMed:8789948). Detected throughout the brain, and in brain stem trigeminal nucleus (PubMed:8789948). Detected in forebrain (PubMed:1377365).2 Publications

Interactioni

Subunit structurei

Heterotetramer. Forms heterotetrameric channels composed of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A, GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:1377365, PubMed:26912815). Can also form heterotetrameric channels that contain at least one zeta subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B (PubMed:12008020, PubMed:14602821). In vivo, the subunit composition may depend on the expression levels of the different subunits (Probable). Found in a complex with GRIN1, GRIN3A and PPP2CB (By similarity). Found in a complex with GRIN1 and GRIN3B (PubMed:12008020, PubMed:14602821). Interacts with MAGI3 (By similarity). Interacts with HIP1 and NETO1 (PubMed:17329427, PubMed:19243221). Interacts with PDZ domains of PATJ, DLG3 and DLG4. Interacts with DAPK1 (PubMed:20141836). Found in a complex with GRIN1 and PRR7. Interacts with PRR7 (By similarity). Interacts with CAMK2A (By similarity).By similarity7 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200069, 76 interactors
ComplexPortaliCPX-291 NMDA receptor complex, GluN1-GluN2B
CPX-296 NMDA receptor complex, GluN1-GluN2A-GluN2B
CORUMiQ01097
DIPiDIP-31568N
IntActiQ01097, 194 interactors
MINTiQ01097
STRINGi10090.ENSMUSP00000062284

Structurei

3D structure databases

ProteinModelPortaliQ01097
SMRiQ01097
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni604 – 623Pore-formingBy similarityAdd BLAST20
Regioni690 – 691Glutamate bindingBy similarity2
Regioni1292 – 1304Interaction with DAPK11 PublicationAdd BLAST13

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1480 – 1482PDZ-bindingBy similarity3

Compositional bias

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

Domaini

A hydrophobic region that gives rise to the prediction of a transmembrane span does not cross the membrane, but is part of a discontinuously helical region that dips into the membrane and is probably part of the pore and of the selectivity filter.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1053 Eukaryota
ENOG410XNUR LUCA
HOGENOMiHOG000113802
HOVERGENiHBG052635
InParanoidiQ01097
KOiK05210
PhylomeDBiQ01097

Family and domain databases

InterProiView protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR019594 Glu/Gly-bd
IPR001508 Iono_rcpt_met
IPR001320 Iontro_rcpt
IPR018884 NMDAR2_C
IPR028082 Peripla_BP_I
PfamiView protein in Pfam
PF01094 ANF_receptor, 1 hit
PF00060 Lig_chan, 1 hit
PF10613 Lig_chan-Glu_bd, 1 hit
PF10565 NMDAR2_C, 1 hit
PRINTSiPR00177 NMDARECEPTOR
SMARTiView protein in SMART
SM00918 Lig_chan-Glu_bd, 1 hit
SM00079 PBPe, 1 hit
SUPFAMiSSF53822 SSF53822, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

Q01097-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKPSAECCSP KFWLVLAVLA VSGSKARSQK SAPSIGIAVI LVGTSDEVAI
60 70 80 90 100
KDAHEKDDFH HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVLA
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 HGTGDKHGVV GGVPAPWEKN
1210 1220 1230 1240 1250
LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN
1260 1270 1280 1290 1300
LYDISEDNSL QELDQPAAPV AVSSNASTTK YPQSPTNSKA QKKNRNKLRR
1310 1320 1330 1340 1350
QHSYDTFVDL QKEEAALAPR SVSLKDKGRF MDGSPYAHMF EMPAGESSFA
1360 1370 1380 1390 1400
NKSSVTTAGH HHNNPGSGYM LSKSLYPDRV TQNPFIPTFG DDQCLLHGSK
1410 1420 1430 1440 1450
SYFFRQPTVA GASKTRPDFR ALVTNKPVVS ALHGAVPGRF QKDICIGNQS
1460 1470 1480
NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV
Length:1,482
Mass (Da):165,959
Last modified:June 20, 2001 - v3
Checksum:iB8C3FA10E9A4B36D
GO

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3X9V4G3X9V4_MOUSE
Glutamate receptor ionotropic, NMDA...
Grin2b mCG_145739
1,482Annotation score:
A0A0G2JEA7A0A0G2JEA7_MOUSE
Glutamate receptor ionotropic, NMDA...
Grin2b
337Annotation score:
Q8CG69Q8CG69_MOUSE
Glutamate receptor ionotropic, NMDA...
Grin2b
35Annotation score:
A0A087WR33A0A087WR33_MOUSE
Glutamate receptor ionotropic, NMDA...
Grin2b
36Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti99L → F in BAB22483 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10651 mRNA Translation: BAA01498.2
AK002963 mRNA Translation: BAB22483.1
CCDSiCCDS20648.1
PIRiI49704
RefSeqiNP_032197.3, NM_008171.3
UniGeneiMm.436649

Genome annotation databases

GeneIDi14812
KEGGimmu:14812

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10651 mRNA Translation: BAA01498.2
AK002963 mRNA Translation: BAB22483.1
CCDSiCCDS20648.1
PIRiI49704
RefSeqiNP_032197.3, NM_008171.3
UniGeneiMm.436649

3D structure databases

ProteinModelPortaliQ01097
SMRiQ01097
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200069, 76 interactors
ComplexPortaliCPX-291 NMDA receptor complex, GluN1-GluN2B
CPX-296 NMDA receptor complex, GluN1-GluN2A-GluN2B
CORUMiQ01097
DIPiDIP-31568N
IntActiQ01097, 194 interactors
MINTiQ01097
STRINGi10090.ENSMUSP00000062284

Chemistry databases

ChEMBLiCHEMBL3442

PTM databases

iPTMnetiQ01097
PhosphoSitePlusiQ01097
SwissPalmiQ01097

Proteomic databases

MaxQBiQ01097
PaxDbiQ01097
PRIDEiQ01097

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi14812
KEGGimmu:14812

Organism-specific databases

CTDi2904
MGIiMGI:95821 Grin2b

Phylogenomic databases

eggNOGiKOG1053 Eukaryota
ENOG410XNUR LUCA
HOGENOMiHOG000113802
HOVERGENiHBG052635
InParanoidiQ01097
KOiK05210
PhylomeDBiQ01097

Miscellaneous databases

PROiPR:Q01097
SOURCEiSearch...

Family and domain databases

InterProiView protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR019594 Glu/Gly-bd
IPR001508 Iono_rcpt_met
IPR001320 Iontro_rcpt
IPR018884 NMDAR2_C
IPR028082 Peripla_BP_I
PfamiView protein in Pfam
PF01094 ANF_receptor, 1 hit
PF00060 Lig_chan, 1 hit
PF10613 Lig_chan-Glu_bd, 1 hit
PF10565 NMDAR2_C, 1 hit
PRINTSiPR00177 NMDARECEPTOR
SMARTiView protein in SMART
SM00918 Lig_chan-Glu_bd, 1 hit
SM00079 PBPe, 1 hit
SUPFAMiSSF53822 SSF53822, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiNMDE2_MOUSE
AccessioniPrimary (citable) accession number: Q01097
Secondary accession number(s): Q9DCB2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 20, 2001
Last modified: November 7, 2018
This is version 186 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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Main funding by: National Institutes of Health

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