Grin2b
entrez
24410
canonical
uniprot
Q00960
canonical
ensembl
ENSRNOG00000008766
resolver
ensp
ENSRNOP00000011697
resolver
ensp
ENSRNOP00000102212
resolver
enst
ENSRNOT00000011697
resolver
enst
ENSRNOT00000159969
resolver
genesymbol
Grin2b
resolver
uniprot
A0ABK0LAK0
resolver
uniprot
G3V746
resolver
uniprot
Q62684
resolver
uniprot_entry
A0ABK0LAK0_RAT
resolver
uniprot_entry
G3V746_RAT
resolver
uniprot_entry
NMDE2_RAT
resolver
uniprot_sec
Q62684
resolver
activity_regulation
ACTIVITY REGULATION: NMDA glutamate receptor activity is inhibited by micromolar levels of zinc ions (PubMed:19910922, PubMed:24607230). NMDA glutamate receptor activity is inhibited by ifenprodil (PubMed:19910922, PubMed:21677647). {ECO:0000269|PubMed:19910922, ECO:0000269|PubMed:21677647, ECO:0000269|PubMed:24607230}.
uniprot
proteins
amino_acid_sequence
MKPSAECCSPKFWLVLAVLAVSGSKARSQKSPPSIGIAVILVGTSDEVAIKDAHEKDDFHHLSVVPRVELVAMNETDPKSIITRICDLMSDRKIQGVVFADDTDQEAIAQILDFISAQTLTPILGIHGGSSMIMADKDESSMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFVNKIRSTIENSFVGWELEEVLLLDMSLDDGDSKIQNQLKKLQSPIILLYCTKEEATYIFEVANSVGLTGYGYTWIVPSLVAGDTDTVPSEFPTGLISVSYDEWDYGLPARVRDGIAIITTAASDMLSEHSFIPEPKSSCYNTHEKRIYQSNMLNRYLINVTFEGRNLSFSEDGYQMHPKLVIILLNKERKWERVGKWKDKSLQMKYYVWPRMCPETEEQEDDHLSIVTLEEAPFVIVESVDPLSGTCMRNTVPCQKRIISENKTDEEPGYIKKCCKGFCIDILKKISKSVKFTYDLYLVTNGKHGKKINGTWNGMIGEVVMKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSRSNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYVDQVSGLSDKKFQRPNDFSPPFRFGTVPNGSTERNIRNNYAEMHAYMGKFNQRGVDDALLSLKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLGAAMALSLITFICEHLFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSVMNSPTATMNNTHSNILRLLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSYNNPPCEENLFSDYISEVERTFGNLQLKDSNVYQDHYHHHHRPHSIGSTSSIDGLYDCDNPPFTTQPRSISKKPLDIGLPSSKHSQLSDLYGKFSFKSDRYSGHDDLIRSDVSDISTHTVTYGNIEGNAAKRRKQQYKDSLKKRPASAKSRREFDEIELAYRRRPPRSPDHKRYFRDKEGLRDFYLDQFRTKENSPHWEHVDLTDIYKERSDDFKRDSVSGGGPCTNRSHLKHGTGEKHGVVGGVPAPWEKNLTNVDWEDRSGGNFCRSCPSKLHNYSSTVAGQNSGRQACIRCEACKKAGNLYDISEDNSLQELDQPAAPVAVTSNASSTKYPQSPTNSKAQKKNRNKLRRQHSYDTFVDLQKEEAALAPRSVSLKDKGRFMDGSPYAHMFEMPAGESSFANKSSVPTAGHHHNNPGSGYMLSKSLYPDRVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVAGASKTRPDFRALVTNKPVVVTLHGAVPGRFQKDICIGNQSNPCVPNNKNPRAFNGSSNGHVYEKLSSIESDV
uniprot
proteins
function
FUNCTION: Component of N-methyl-D-aspartate (NMDA) receptors (NMDARs) that function as heterotetrameric, ligand-gated cation channels with high calcium permeability and voltage-dependent block by Mg(2+) (PubMed:11929923, PubMed:19910922, PubMed:21677647, PubMed:24607230, PubMed:24876489, PubMed:27135925, PubMed:7524561). Participates in synaptic plasticity for learning and memory formation by contributing to the long-term depression (LTD) of hippocampus membrane currents (By similarity). Channel activation requires binding of the neurotransmitter L-glutamate to the GluN2 subunit, glycine or D-serine binding to the GluN1 subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:11929923, PubMed:19910922, PubMed:21677647, PubMed:24607230, PubMed:24876489, PubMed:27135925, PubMed:7524561). NMDARs mediate simultaneously the potassium efflux and the influx of calcium and sodium (By similarity). Each GluN2 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (PubMed:10436042, PubMed:11929923, PubMed:24607230, PubMed:9463421). In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage (By similarity). 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). {ECO:0000250|UniProtKB:P35438, ECO:0000250|UniProtKB:Q01097, ECO:0000269|PubMed:10436042, ECO:0000269|PubMed:11929923, ECO:0000269|PubMed:19910922, ECO:0000269|PubMed:21677647, ECO:0000269|PubMed:24607230, ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925, ECO:0000269|PubMed:7524561, ECO:0000269|PubMed:9463421}.
uniprot
proteins
mass_dalton
166071
uniprot
proteins
mutagenesis
MUTAGEN 60; /note="H->A: Normal zinc binding."; /evidence="ECO:0000269|PubMed:19910922"; MUTAGEN 127; /note="H->A: Reduced zinc binding."; /evidence="ECO:0000269|PubMed:19910922"; MUTAGEN 283; /note="D->A: Slightly reduced zinc binding."; /evidence="ECO:0000269|PubMed:19910922"; MUTAGEN 284; /note="E->A: Reduced zinc binding."; /evidence="ECO:0000269|PubMed:19910922"; MUTAGEN 311; /note="H->A: Normal zinc binding."; /evidence="ECO:0000269|PubMed:19910922"; MUTAGEN 359; /note="H->A: Normal zinc binding."; /evidence="ECO:0000269|PubMed:19910922"; MUTAGEN 1413; /note="S->L: Decreased localization to the cell membrane. Decreased interaction with DLG3 and DLG4. No effect on glutamate-gated calcium ion channel activity."; /evidence="ECO:0000269|PubMed:28283559"; MUTAGEN 1422; /note="L->F: No effect on localizationto the cell membrane. Decreased interaction with DLG3 and DLG4. No effect on glutamate-gated calcium ion channel activity."; /evidence="ECO:0000269|PubMed:28283559"; MUTAGEN 1450; /note="S->F: No effect on localizationto the cell membrane. Decreased interaction with DLG3 and DLG4. No effect on glutamate-gated calcium ion channel activity."; /evidence="ECO:0000269|PubMed:28283559
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues (PubMed:7513428). Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity (By similarity). {ECO:0000250|UniProtKB:Q01097, ECO:0000269|PubMed:7513428}.
uniprot
proteins
protein_family
Glutamate-gated ion channel (TC 1.A.10.1) family
uniprot
proteins
protein_family
NR2B/GRIN2B subfamily
uniprot
proteins
pubmed
10436042
uniprot
proteins
pubmed
11588171
uniprot
proteins
pubmed
11929923
uniprot
proteins
pubmed
12391275
uniprot
proteins
pubmed
1350383
uniprot
proteins
pubmed
19910922
uniprot
proteins
pubmed
21677647
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
22960932
uniprot
proteins
pubmed
24607230
uniprot
proteins
pubmed
24876489
uniprot
proteins
pubmed
27135925
uniprot
proteins
pubmed
27458189
uniprot
proteins
pubmed
27916457
uniprot
proteins
pubmed
28283559
uniprot
proteins
pubmed
31080121
uniprot
proteins
pubmed
7513428
uniprot
proteins
pubmed
7524561
uniprot
proteins
pubmed
7569905
uniprot
proteins
pubmed
9463421
uniprot
proteins
pubmed
9509416
uniprot
proteins
pubmed
9647694
uniprot
proteins
sequence_length
1482
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1350383, ECO:0000269|PubMed:19910922, ECO:0000269|PubMed:21677647, ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925, ECO:0000269|PubMed:27916457}; Multi-pass membrane protein {ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925}. Postsynaptic cell membrane {ECO:0000269|PubMed:7513428, ECO:0000269|PubMed:9509416}; Multi-pass membrane protein {ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925}. Late endosome {ECO:0000250|UniProtKB:Q01097}. Lysosome {ECO:0000250|UniProtKB:Q01097}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q01097}. Note=Co-localizes with the motor protein KIF17 along microtubules. {ECO:0000250|UniProtKB:Q01097}.
uniprot
proteins
transmembrane_region
TRANSMEM 558..576; /note="Helical"; /evidence="ECO:0000269|PubMed:24876489"; TRANSMEM 631..646; /note="Helical"; /evidence="ECO:0000269|PubMed:24876489"; TRANSMEM 818..837; /note="Helical"; /evidence="ECO:0000269|PubMed:24876489
uniprot
proteins