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Protein

Glutamate receptor ionotropic, NMDA 2B

Gene

GRIN2B

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi127 – 1271ZincBy similarity
Metal bindingi284 – 2841ZincBy similarity
Sitei615 – 6151Functional determinant of NMDA receptorsBy similarity

GO - Molecular functioni

GO - Biological processi

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-CFA-3928662. EPHB-mediated forward signaling.
R-CFA-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-CFA-442729. CREB phosphorylation through the activation of CaMKII.
R-CFA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-CFA-5673001. RAF/MAP kinase cascade.
R-CFA-8849932. SALM protein interactions at the synapse.

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
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Chromosome 27

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 557531ExtracellularSequence analysisAdd
BLAST
Transmembranei558 – 57821HelicalSequence analysisAdd
BLAST
Topological domaini579 – 63456CytoplasmicSequence analysisAdd
BLAST
Transmembranei635 – 65521HelicalSequence analysisAdd
BLAST
Topological domaini656 – 817162ExtracellularSequence analysisAdd
BLAST
Transmembranei818 – 83821HelicalSequence analysisAdd
BLAST
Topological domaini839 – 1485647CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 14851459Glutamate receptor ionotropic, NMDA 2BPRO_0000289579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence analysis
Disulfide bondi86 ↔ 321By similarity
Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence analysis
Glycosylationi348 – 3481N-linked (GlcNAc...)Sequence analysis
Glycosylationi444 – 4441N-linked (GlcNAc...)Sequence analysis
Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence analysis
Glycosylationi542 – 5421N-linked (GlcNAc...)Sequence analysis
Glycosylationi688 – 6881N-linked (GlcNAc...)Sequence analysis
Modified residuei882 – 8821PhosphoserineBy similarity
Modified residuei886 – 8861PhosphoserineBy similarity
Modified residuei917 – 9171PhosphoserineBy similarity
Modified residuei920 – 9201PhosphoserineBy similarity
Modified residuei962 – 9621PhosphotyrosineBy similarity
Modified residuei1039 – 10391PhosphotyrosineBy similarity
Modified residuei1058 – 10581PhosphoserineBy similarity
Modified residuei1061 – 10611PhosphoserineBy similarity
Modified residuei1064 – 10641PhosphoserineBy similarity
Modified residuei1109 – 11091PhosphotyrosineBy similarity
Modified residuei1133 – 11331PhosphotyrosineBy similarity
Modified residuei1143 – 11431PhosphoserineBy similarity
Modified residuei1155 – 11551PhosphotyrosineBy similarity
Modified residuei1255 – 12551PhosphoserineBy similarity
Modified residuei1259 – 12591PhosphoserineBy similarity
Modified residuei1303 – 13031Phosphoserine; by DAPK1By similarity
Modified residuei1475 – 14751PhosphotyrosineBy similarity

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

PaxDbiQ5R1P3.
PRIDEiQ5R1P3.

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 INADL, DLG4 and MAGI3. Interacts with HIP1 and NETO1 (By similarity). Interacts with DAPK1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000039796.

Structurei

3D structure databases

ProteinModelPortaliQ5R1P3.
SMRiQ5R1P3. Positions 404-802.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1292 – 130413Interaction with DAPK1By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1483 – 14853PDZ-bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi984 – 9896Poly-His

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
GeneTreeiENSGT00760000119186.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ5R1P3.
KOiK05210.
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.

Q5R1P3-1 [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 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 VSENKTDEEP
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 FTTQPRSISK KPLDLGLPSS 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
LTDIYKEQSD DFKRDSVSGG GPCTNRSHLK HGAGDKHGVV SGVPAPWEKN
1210 1220 1230 1240 1250
LSNVDWEDRS GGNFCRSCPS KLHNYSTAVT GQNSGRQACI RCEACKKAGN
1260 1270 1280 1290 1300
LYDISEDNSL QELDQPAAPV AVPSNAPSTK YPQSPTNSKA QKKTRNKLRR
1310 1320 1330 1340 1350
QHSYDTFVDL QKEEAALAPR SVSLKDKGRF LDGSPYAHMF ETPAGESTFA
1360 1370 1380 1390 1400
NHESSVAAAG HRHHNNPGGG GYMLSKSLYP DRVTQNPFIP TFGDDQCLLH
1410 1420 1430 1440 1450
GSKSYFFRQP TVAGAPKARP DFRALVTNKP VVSALHGAVP GRFQKDICIG
1460 1470 1480
NQSNPCVPNN KNPRAFNGSS NGHVYEKLSS IESDV
Length:1,485
Mass (Da):166,244
Last modified:January 4, 2005 - v1
Checksum:i526E5868F98BDE1D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB195992 mRNA. Translation: BAD74215.1.
RefSeqiNP_001008719.1. NM_001008719.1.
XP_005636773.1. XM_005636716.2.
XP_013963742.1. XM_014108267.1.
XP_013963743.1. XM_014108268.1.
UniGeneiCfa.16222.

Genome annotation databases

EnsembliENSCAFT00000020886; ENSCAFP00000019393; ENSCAFG00000013148.
GeneIDi494009.
KEGGicfa:494009.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB195992 mRNA. Translation: BAD74215.1.
RefSeqiNP_001008719.1. NM_001008719.1.
XP_005636773.1. XM_005636716.2.
XP_013963742.1. XM_014108267.1.
XP_013963743.1. XM_014108268.1.
UniGeneiCfa.16222.

3D structure databases

ProteinModelPortaliQ5R1P3.
SMRiQ5R1P3. Positions 404-802.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000039796.

Proteomic databases

PaxDbiQ5R1P3.
PRIDEiQ5R1P3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000020886; ENSCAFP00000019393; ENSCAFG00000013148.
GeneIDi494009.
KEGGicfa:494009.

Organism-specific databases

CTDi2904.

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
GeneTreeiENSGT00760000119186.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ5R1P3.
KOiK05210.
TreeFamiTF314731.

Enzyme and pathway databases

ReactomeiR-CFA-3928662. EPHB-mediated forward signaling.
R-CFA-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-CFA-442729. CREB phosphorylation through the activation of CaMKII.
R-CFA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-CFA-5673001. RAF/MAP kinase cascade.
R-CFA-8849932. SALM protein interactions at the synapse.

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_CANLF
AccessioniPrimary (citable) accession number: Q5R1P3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: January 4, 2005
Last modified: July 6, 2016
This is version 89 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

Complete proteome, Reference proteome

Documents

  1. 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.