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Q00960

- NMDE2_RAT

UniProt

Q00960 - NMDE2_RAT

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Protein
Glutamate receptor ionotropic, NMDA 2B
Gene
Grin2b
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi127 – 1271Zinc
Metal bindingi284 – 2841Zinc
Sitei615 – 6151Functional determinant of NMDA receptors By similarity

GO - Molecular functioni

  1. D2 dopamine receptor binding Source: RGD
  2. N-methyl-D-aspartate selective glutamate receptor activity Source: RGD
  3. beta-catenin binding Source: RGD
  4. cell adhesion molecule binding Source: RGD
  5. drug binding Source: RGD
  6. extracellular-glutamate-gated ion channel activity Source: RGD
  7. interleukin-1 receptor binding Source: RGD
  8. ionotropic glutamate receptor activity Source: RGD
  9. ionotropic glutamate receptor binding Source: RGD
  10. neurotransmitter binding Source: RGD
  11. protein binding Source: UniProtKB
  12. protein heterodimerization activity Source: RGD
  13. receptor binding Source: RGD
  14. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. action potential Source: RGD
  2. associative learning Source: RGD
  3. cellular response to amino acid stimulus Source: RGD
  4. cellular response to dsRNA Source: RGD
  5. cellular response to growth factor stimulus Source: RGD
  6. cellular response to lipid Source: RGD
  7. cellular response to magnesium starvation Source: RGD
  8. cellular response to manganese ion Source: RGD
  9. cellular response to organic cyclic compound Source: RGD
  10. cerebral cortex development Source: RGD
  11. hippocampus development Source: RGD
  12. ion transmembrane transport Source: GOC
  13. ionotropic glutamate receptor signaling pathway Source: RGD
  14. learning or memory Source: RGD
  15. long-term memory Source: RGD
  16. memory Source: UniProtKB
  17. multicellular organismal response to stress Source: RGD
  18. positive regulation of cell death Source: RGD
  19. positive regulation of glutamate secretion Source: UniProtKB
  20. positive regulation of synaptic transmission Source: RGD
  21. receptor clustering Source: RGD
  22. regulation of MAPK cascade Source: UniProtKB
  23. regulation of long-term neuronal synaptic plasticity Source: RGD
  24. response to acid Source: RGD
  25. response to amine Source: RGD
  26. response to amphetamine Source: RGD
  27. response to calcium ion Source: RGD
  28. response to carbohydrate Source: RGD
  29. response to cocaine Source: RGD
  30. response to cytokine Source: RGD
  31. response to electrical stimulus Source: RGD
  32. response to ethanol Source: RGD
  33. response to fungicide Source: RGD
  34. response to growth hormone Source: RGD
  35. response to magnesium ion Source: RGD
  36. response to manganese ion Source: RGD
  37. response to mechanical stimulus Source: RGD
  38. response to methylmercury Source: RGD
  39. response to organic cyclic compound Source: RGD
  40. response to other organism Source: RGD
  41. rhythmic process Source: RGD
  42. synaptic transmission, glutamatergic Source: RefGenome
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

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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2738. Grin2b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 557531Extracellular Reviewed prediction
Add
BLAST
Transmembranei558 – 57821Helical; Reviewed prediction
Add
BLAST
Topological domaini579 – 63456Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei635 – 65521Helical; Reviewed prediction
Add
BLAST
Topological domaini656 – 817162Extracellular Reviewed prediction
Add
BLAST
Transmembranei818 – 83821Helical; Reviewed prediction
Add
BLAST
Topological domaini839 – 1482644Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. N-methyl-D-aspartate selective glutamate receptor complex Source: UniProtKB
  2. Z disc Source: RGD
  3. cell junction Source: UniProtKB-KW
  4. dendritic spine Source: RGD
  5. neuron projection Source: UniProtKB
  6. postsynaptic density Source: RGD
  7. postsynaptic membrane Source: RefGenome
  8. presynaptic membrane Source: UniProtKB
  9. synapse Source: UniProtKB
  10. synaptic cleft Source: RGD
  11. terminal bouton Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601H → A: Normal zinc binding. 1 Publication
Mutagenesisi127 – 1271H → A: Reduced zinc binding.
Mutagenesisi283 – 2831D → A: Slightly reduced zinc binding.
Mutagenesisi284 – 2841E → A: Reduced zinc binding.
Mutagenesisi311 – 3111H → A: Normal zinc binding. 1 Publication
Mutagenesisi359 – 3591H → A: Normal zinc binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626 Reviewed prediction
Add
BLAST
Chaini27 – 14821456Glutamate receptor ionotropic, NMDA 2B
PRO_0000011579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)1 Publication
Disulfide bondi86 ↔ 3211 Publication
Glycosylationi341 – 3411N-linked (GlcNAc...)1 Publication
Glycosylationi348 – 3481N-linked (GlcNAc...) Reviewed prediction
Glycosylationi444 – 4441N-linked (GlcNAc...) Reviewed prediction
Glycosylationi491 – 4911N-linked (GlcNAc...) Reviewed prediction
Glycosylationi542 – 5421N-linked (GlcNAc...) Reviewed prediction
Glycosylationi688 – 6881N-linked (GlcNAc...) Reviewed prediction
Modified residuei962 – 9621Phosphotyrosine By similarity
Modified residuei1039 – 10391Phosphotyrosine By similarity
Modified residuei1109 – 11091Phosphotyrosine By similarity
Modified residuei1133 – 11331Phosphotyrosine By similarity
Modified residuei1155 – 11551Phosphotyrosine By similarity
Modified residuei1303 – 13031Phosphoserine; by DAPK1 By similarity
Modified residuei1472 – 14721Phosphotyrosine By 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

PaxDbiQ00960.
PRIDEiQ00960.

PTM databases

PhosphoSiteiQ00960.

Expressioni

Gene expression databases

GenevestigatoriQ00960.

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 INADL and DLG4. Interacts with DAPK1 By similarity.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
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

Protein-protein interaction databases

BioGridi246575. 11 interactions.
DIPiDIP-33702N.
IntActiQ00960. 16 interactions.
MINTiMINT-104014.
STRINGi10116.ENSRNOP00000011697.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 4411
Helixi47 – 504
Helixi53 – 553
Beta strandi64 – 7310
Helixi78 – 9114
Beta strandi94 – 10310
Helixi107 – 11913
Beta strandi123 – 1275
Helixi128 – 1314
Beta strandi143 – 1475
Helixi150 – 16314
Beta strandi168 – 1758
Helixi179 – 19113
Beta strandi198 – 2058
Beta strandi211 – 2133
Helixi215 – 2206
Beta strandi226 – 2327
Helixi234 – 24512
Turni246 – 2483
Beta strandi250 – 2534
Beta strandi255 – 2584
Helixi260 – 2634
Beta strandi275 – 2817
Turni284 – 2863
Helixi289 – 30820
Turni309 – 3113
Turni322 – 3265
Helixi327 – 3304
Helixi336 – 3394
Beta strandi355 – 3595
Beta strandi362 – 3676
Beta strandi369 – 3713
Beta strandi373 – 3797
Beta strandi384 – 3874

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ00960.
SMRiQ00960. Positions 404-802.

Miscellaneous databases

EvolutionaryTraceiQ00960.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1292 – 130413Interaction with DAPK1 By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1480 – 14823PDZ-binding

Compositional bias

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

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG282132.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ00960.
KOiK05210.
PhylomeDBiQ00960.

Family and domain databases

InterProiIPR001828. 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]
PfamiPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10565. NMDAR2_C. 1 hit.
PF00497. SBP_bac_3. 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

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MKPSAECCSP KFWLVLAVLA VSGSKARSQK SPPSIGIAVI LVGTSDEVAI     50
KDAHEKDDFH HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVFA 100
DDTDQEAIAQ ILDFISAQTL TPILGIHGGS SMIMADKDES SMFFQFGPSI 150
EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ DFVNKIRSTI ENSFVGWELE 200
EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI FEVANSVGLT 250
GYGYTWIVPS LVAGDTDTVP SEFPTGLISV SYDEWDYGLP ARVRDGIAII 300
TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS 350
FSEDGYQMHP KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE 400
QEDDHLSIVT LEEAPFVIVE SVDPLSGTCM RNTVPCQKRI ISENKTDEEP 450
GYIKKCCKGF CIDILKKISK SVKFTYDLYL VTNGKHGKKI NGTWNGMIGE 500
VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR SNGTVSPSAF 550
LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF 600
TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL 650
AAFMIQEEYV DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA 700
EMHAYMGKFN QRGVDDALLS LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT 750
IGSGKVFAST GYGIAIQKDS GWKRQVDLAI LQLFGDGEME ELEALWLTGI 800
CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH LFYWQFRHCF 850
MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR 900
LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN 950
NPPCEENLFS DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSTSSI 1000
DGLYDCDNPP FTTQPRSISK KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS 1050
GHDDLIRSDV SDISTHTVTY GNIEGNAAKR RKQQYKDSLK KRPASAKSRR 1100
EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK ENSPHWEHVD 1150
LTDIYKERSD DFKRDSVSGG GPCTNRSHLK HGTGEKHGVV GGVPAPWEKN 1200
LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN 1250
LYDISEDNSL QELDQPAAPV AVTSNASSTK YPQSPTNSKA QKKNRNKLRR 1300
QHSYDTFVDL QKEEAALAPR SVSLKDKGRF MDGSPYAHMF EMPAGESSFA 1350
NKSSVPTAGH HHNNPGSGYM LSKSLYPDRV TQNPFIPTFG DDQCLLHGSK 1400
SYFFRQPTVA GASKTRPDFR ALVTNKPVVV TLHGAVPGRF QKDICIGNQS 1450
NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV 1482
Length:1,482
Mass (Da):166,071
Last modified:June 1, 1994 - v1
Checksum:iAEF8B9DF3C1B0D5D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1256 – 12561E → K in AAA50554. 1 Publication
Sequence conflicti1430 – 14312VT → SA in AAA50554. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M91562 mRNA. Translation: AAA41714.1 .
U11419 mRNA. Translation: AAA50554.1 .
PIRi B43274.
RefSeqi NP_036706.1. NM_012574.1.
UniGenei Rn.9711.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3JPW X-ray 2.80 A 32-394 [» ]
3JPY X-ray 3.21 A 32-394 [» ]
3QEL X-ray 2.60 B/D 31-394 [» ]
3QEM X-ray 3.00 B/D 31-394 [» ]
4PE5 X-ray 3.96 B/D 27-852 [» ]
ProteinModelPortali Q00960.
SMRi Q00960. Positions 404-802.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246575. 11 interactions.
DIPi DIP-33702N.
IntActi Q00960. 16 interactions.
MINTi MINT-104014.
STRINGi 10116.ENSRNOP00000011697.

Chemistry

BindingDBi Q00960.
ChEMBLi CHEMBL2096669.
GuidetoPHARMACOLOGYi 457.

Protein family/group databases

TCDBi 1.A.10.1.6. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSitei Q00960.

Proteomic databases

PaxDbi Q00960.
PRIDEi Q00960.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24410.
KEGGi rno:24410.
UCSCi RGD:2738. rat.

Organism-specific databases

CTDi 2904.
RGDi 2738. Grin2b.

Phylogenomic databases

eggNOGi NOG282132.
HOGENOMi HOG000113802.
HOVERGENi HBG052635.
InParanoidi Q00960.
KOi K05210.
PhylomeDBi Q00960.

Miscellaneous databases

EvolutionaryTracei Q00960.
NextBioi 603231.
PROi Q00960.

Gene expression databases

Genevestigatori Q00960.

Family and domain databases

InterProi IPR001828. 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 ]
Pfami PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10565. NMDAR2_C. 1 hit.
PF00497. SBP_bac_3. 1 hit.
[Graphical view ]
PRINTSi PR00177. NMDARECEPTOR.
SMARTi SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view ]
SUPFAMi SSF53822. SSF53822. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Heteromeric NMDA receptors: molecular and functional distinction of subtypes."
    Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H., Burnashev N., Sakmann B., Seeburg P.H.
    Science 256:1217-1221(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor."
    Sullivan J.M., Traynelis S.F., Chen H.S., Escobar W., Heinemann S.F., Lipton S.A.
    Neuron 13:929-936(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95."
    Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H.
    Science 269:1737-1740(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DLG4.
  4. "CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins."
    Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.
    Mol. Cell. Neurosci. 11:161-172(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INADL.
  5. "An NMDA receptor signaling complex with protein phosphatase 2A."
    Chan S.F., Sucher N.J.
    J. Neurosci. 21:7985-7992(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN3A AND PPP2CB.
  6. "Assembly with the NR1 subunit is required for surface expression of NR3A-containing NMDA receptors."
    Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A., Trimmer J.S., Sucher N.J., Heinemann S.F.
    J. Neurosci. 21:1228-1237(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
  7. "Association of NR3A with the N-methyl-D-aspartate receptor NR1 and NR2 subunits."
    Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B., Yasuda R.P.
    Mol. Pharmacol. 62:1119-1127(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
  8. "Characterization and comparison of the NR3A subunit of the NMDA receptor in recombinant systems and primary cortical neurons."
    Sasaki Y.F., Rothe T., Premkumar L.S., Das S., Cui J., Talantova M.V., Wong H.-K., Gong X., Chan S.F., Zhang D., Nakanishi N., Sucher N.J., Lipton S.A.
    J. Neurophysiol. 87:2052-2063(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
  9. "Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit."
    Karakas E., Simorowski N., Furukawa H.
    EMBO J. 28:3910-3920(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 32-394 IN COMPLEX WITH ZINC ION, GLYCOSYLATION AT ASN-74; HIS-127; ASP-283; GLU-284 AND ASN-341, MUTAGENESIS OF HIS-60; HIS-311 AND HIS-359, DISULFIDE BOND.

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: September 3, 2014
This is version 142 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

External Data

Dasty 3

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