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Q01097 (NMDE2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. 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

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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.12

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 and GRIN3B. Found in a complex with GRIN1, GRIN3A and PPP2CB. Interacts with PDZ domains of INADL, DLG4 and MAGI3 By similarity. Interacts with HIP1 and NETO1. Interacts with DAPK1. Ref.5 Ref.6 Ref.8 Ref.11 Ref.12

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein.

Post-translational modification

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

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 termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral fear response

Inferred from mutant phenotype PubMed 16710293. Source: MGI

behavioral response to pain

Inferred from mutant phenotype PubMed 11711849. Source: MGI

calcium ion transmembrane transport

Inferred from mutant phenotype PubMed 12816890. Source: GOC

calcium ion transport

Inferred from mutant phenotype PubMed 12816890PubMed 16045501. Source: MGI

cation transport

Inferred from genetic interaction PubMed 7531804. Source: MGI

detection of mechanical stimulus involved in sensory perception of pain

Inferred from mutant phenotype PubMed 16190898. Source: MGI

fear response

Inferred from mutant phenotype PubMed 16157280. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 9147327. Source: MGI

ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: GOC

ionotropic glutamate receptor signaling pathway

Inferred from mutant phenotype PubMed 10634899PubMed 12816890PubMed 12832518PubMed 9458051. Source: GOC

learning

Inferred from direct assay PubMed 10485705. Source: MGI

learning or memory

Traceable author statement PubMed 14622581. Source: UniProtKB

memory

Inferred from direct assay PubMed 10485705. Source: MGI

regulation of excitatory postsynaptic membrane potential

Inferred from mutant phenotype PubMed 10634899PubMed 11530236PubMed 12832518PubMed 16045501PubMed 16157280PubMed 9147327. Source: MGI

regulation of neuronal synaptic plasticity

Traceable author statement PubMed 14622581. Source: UniProtKB

regulation of postsynaptic membrane potential

Inferred from mutant phenotype PubMed 16157280. Source: MGI

regulation of synaptic plasticity

Inferred from mutant phenotype PubMed 11719203PubMed 16710293. Source: MGI

response to ethanol

Inferred from mutant phenotype PubMed 11530236. Source: MGI

sensory organ development

Inferred from mutant phenotype PubMed 8789948. Source: MGI

startle response

Inferred from mutant phenotype PubMed 11488959. Source: MGI

suckling behavior

Inferred from mutant phenotype PubMed 8789948. Source: MGI

synaptic transmission

Inferred from mutant phenotype PubMed 8789948. Source: MGI

synaptic transmission, glutamatergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentN-methyl-D-aspartate selective glutamate receptor complex

Inferred from physical interaction PubMed 9003035. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from direct assay PubMed 17229826. Source: BHF-UCL

membrane

Inferred from direct assay PubMed 10846156PubMed 8840015PubMed 9003035. Source: MGI

neuron projection

Inferred from direct assay PubMed 21795692. Source: BHF-UCL

neuronal postsynaptic density

Inferred from direct assay PubMed 21664258. Source: BHF-UCL

postsynaptic density

Inferred from direct assay PubMed 15748150PubMed 16190898. Source: MGI

postsynaptic membrane

Inferred from direct assay PubMed 12890763. Source: MGI

presynaptic membrane

Inferred from direct assay PubMed 16157280. Source: UniProtKB

synapse

Inferred from direct assay PubMed 14645471PubMed 16710293. Source: MGI

synaptic vesicle

Inferred from direct assay PubMed 10846156PubMed 20418887. Source: MGI

   Molecular_functionN-methyl-D-aspartate selective glutamate receptor activity

Inferred from mutant phenotype PubMed 10634899PubMed 12816890PubMed 12832518PubMed 9458051. Source: MGI

calcium channel activity

Inferred from mutant phenotype PubMed 12816890. Source: MGI

cation channel activity

Inferred from genetic interaction PubMed 7531804. Source: MGI

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction Ref.8Ref.11. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 14821456Glutamate receptor ionotropic, NMDA 2B
PRO_0000011578

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
Motif1480 – 14823PDZ-binding By similarity
Compositional bias984 – 9896Poly-His

Sites

Metal binding1271Zinc By similarity
Metal binding2841Zinc By similarity
Site6151Functional determinant of NMDA receptors By similarity

Amino acid modifications

Modified residue9621Phosphotyrosine Ref.10
Modified residue10391Phosphotyrosine Ref.10
Modified residue11091Phosphotyrosine Ref.10
Modified residue11331Phosphotyrosine Ref.10
Modified residue11551Phosphotyrosine Ref.10
Modified residue13031Phosphoserine; by DAPK1 Ref.12
Modified residue14721Phosphotyrosine Ref.4
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation3411N-linked (GlcNAc...) Potential
Glycosylation3481N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential
Glycosylation5421N-linked (GlcNAc...) Potential
Glycosylation6881N-linked (GlcNAc...) Potential
Disulfide bond86 ↔ 321 By similarity

Experimental info

Sequence conflict991L → F in BAB22483. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q01097 [UniParc].

Last modified June 20, 2001. Version 3.
Checksum: B8C3FA10E9A4B36D

FASTA1,482165,959
        10         20         30         40         50         60 
MKPSAECCSP KFWLVLAVLA VSGSKARSQK SAPSIGIAVI LVGTSDEVAI KDAHEKDDFH 

        70         80         90        100        110        120 
HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVLA 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 HGTGDKHGVV GGVPAPWEKN 

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

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

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

      1390       1400       1410       1420       1430       1440 
TQNPFIPTFG DDQCLLHGSK SYFFRQPTVA GASKTRPDFR ALVTNKPVVS ALHGAVPGRF 

      1450       1460       1470       1480 
QKDICIGNQS NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV 

« Hide

References

« Hide 'large scale' references
[1]"Molecular diversity of the NMDA receptor channel."
Kutsuwada T., Kashiwabuchi N., Mori H., Sakimura K., Kushiya E., Araki K., Meguro H., Masaki H., Kumanishi T., Arakawa M., Mishina M.
Nature 358:36-41(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Kutsuwada T., Kashiwabuchi N., Mori H., Sakimura K., Kushiya E., Araki K., Meguro H., Masaki H., Kumanishi T., Arakawa M., Mishina M.
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-337.
Strain: C57BL/6J.
Tissue: Brain.
[4]"Regulation of NMDA receptor function by Fyn-mediated tyrosine phosphorylation."
Nakazawa T., Tezuka T., Yamamoto T.
Nihon Shinkei Seishin Yakurigaku Zasshi 22:165-167(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-1472.
[5]"Cloning and characterization of a novel NMDA receptor subunit NR3B: a dominant subunit that reduces calcium permeability."
Matsuda K., Kamiya Y., Matsuda S., Yuzaki M.
Brain Res. Mol. Brain Res. 100:43-52(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
[6]"Specific assembly with the NMDA receptor 3B subunit controls surface expression and calcium permeability of NMDA receptors."
Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.
J. Neurosci. 23:10064-10073(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
[7]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[8]"NMDA receptor function and NMDA receptor-dependent phosphorylation of huntingtin is altered by the endocytic protein HIP1."
Metzler M., Gan L., Wong T.P., Liu L., Helm J., Liu L., Georgiou J., Wang Y., Bissada N., Cheng K., Roder J.C., Wang Y.T., Hayden M.R.
J. Neurosci. 27:2298-2308(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIP1.
[9]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[10]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-962; TYR-1039; TYR-1109; TYR-1133 AND TYR-1155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[11]"Neto1 is a novel CUB-domain NMDA receptor-interacting protein required for synaptic plasticity and learning."
Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M., Clapcote S.J., Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M., Roder J.C., Salter M.W., McInnes R.R.
PLoS Biol. 7:E41-E41(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NETO1.
[12]"DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage in stroke."
Tu W., Xu X., Peng L., Zhong X., Zhang W., Soundarapandian M.M., Balel C., Wang M., Jia N., Zhang W., Lew F., Chan S.L., Chen Y., Lu Y.
Cell 140:222-234(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-1303, INTERACTION WITH DAPK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10651 mRNA. Translation: BAA01498.2.
AK002963 mRNA. Translation: BAB22483.1.
CCDSCCDS20648.1.
PIRI49704.
RefSeqNP_032197.3. NM_008171.3.
UniGeneMm.436649.

3D structure databases

ProteinModelPortalQ01097.
SMRQ01097. Positions 33-836.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200069. 71 interactions.
DIPDIP-31568N.
IntActQ01097. 187 interactions.
MINTMINT-135847.

Chemistry

BindingDBQ01097.
ChEMBLCHEMBL3442.
GuidetoPHARMACOLOGY457.

PTM databases

PhosphoSiteQ01097.

Proteomic databases

PaxDbQ01097.
PRIDEQ01097.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID14812.
KEGGmmu:14812.

Organism-specific databases

CTD2904.
MGIMGI:95821. Grin2b.

Phylogenomic databases

eggNOGNOG282132.
HOGENOMHOG000113802.
HOVERGENHBG052635.
InParanoidQ01097.
KOK05210.
PhylomeDBQ01097.

Gene expression databases

GenevestigatorQ01097.

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.
IPR028082. Peripla_BP_I.
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]
SUPFAMSSF53822. SSF53822. 1 hit.
ProtoNetSearch...

Other

NextBio287003.
PROQ01097.
SOURCESearch...

Entry information

Entry nameNMDE2_MOUSE
AccessionPrimary (citable) accession number: Q01097
Secondary accession number(s): Q9DCB2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 20, 2001
Last modified: July 9, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot