Grin1
entrez
14810
canonical
uniprot
P35438
canonical
ensembl
ENSMUSG00000026959
resolver
ensp
ENSMUSP00000028335
resolver
ensp
ENSMUSP00000109946
resolver
ensp
ENSMUSP00000109947
resolver
ensp
ENSMUSP00000109949
resolver
ensp
ENSMUSP00000109951
resolver
ensp
ENSMUSP00000109953
resolver
ensp
ENSMUSP00000109956
resolver
ensp
ENSMUSP00000109957
resolver
enst
ENSMUST00000114307
resolver
enst
ENSMUST00000114308
resolver
enst
ENSMUST00000114310
resolver
enst
ENSMUST00000114314
resolver
enst
ENSMUST00000114317
resolver
enst
ENSMUST00000114318
resolver
genesymbol
Grin1
resolver
genesymbol_syn
Glurz1
resolver
uniprot
A2AI14
resolver
uniprot
A2AI15
resolver
uniprot
A2AI16
resolver
uniprot
A2AI17
resolver
uniprot
A2AI18
resolver
uniprot
A2AI19
resolver
uniprot
A2AI20
resolver
uniprot
A2AI21
resolver
uniprot
Q8CFS4
resolver
uniprot_entry
A2AI14_MOUSE
resolver
uniprot_entry
A2AI16_MOUSE
resolver
uniprot_entry
A2AI17_MOUSE
resolver
uniprot_entry
A2AI19_MOUSE
resolver
uniprot_entry
A2AI20_MOUSE
resolver
uniprot_entry
A2AI21_MOUSE
resolver
uniprot_entry
NMDZ1_MOUSE
resolver
uniprot_sec
A2AI15
resolver
uniprot_sec
A2AI18
resolver
uniprot_sec
Q8CFS4
resolver
amino_acid_sequence
MSTMHLLTFALLFSCSFARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYNWNHIILLVSDDHEGRAAQKRLETLLEERESKAEKVLQFDPGTKNVTALLMEARDLEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGIIGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTMSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGFCVDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDTSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES
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:12008020, PubMed:12860921, PubMed:14602821, PubMed:1532151, PubMed:8060614, PubMed:9049108). NMDARs participate in synaptic plasticity for learning and memory formation by contributing to the long-term potentiation (LTP) (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:12008020, PubMed:1532151, PubMed:7790891, PubMed:8060614). NMDARs mediate simultaneously the potassium efflux and the influx of calcium and sodium (PubMed:12860921). Each GluN2 or GluN3 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (PubMed:12008020, PubMed:14602821). {ECO:0000250|UniProtKB:Q05586, ECO:0000269|PubMed:12008020, ECO:0000269|PubMed:12860921, ECO:0000269|PubMed:14602821, ECO:0000269|PubMed:1532151, ECO:0000269|PubMed:7790891, ECO:0000269|PubMed:8060614, ECO:0000269|PubMed:9049108}.
uniprot
proteins
mass_dalton
105481
uniprot
proteins
mutagenesis
MUTAGEN 481; /note="D->N: Mutant mice exhibit a decrease in anxiety-like behaviors; the effect is mitigated by administration of D-serine or the glycine transporter inhibitor ALX-5407. They also exhibit deficits in social approach, information processing, performance in the Morris water maze, and enhanced startle reactivity. The effects are partially reversed; when associated with 'R-181' in Dao."; /evidence="ECO:0000269|PubMed:18940194, ECO:0000269|PubMed:19751394
uniprot
proteins
post_translational_modification
PTM: NMDA is probably regulated by C-terminal phosphorylation of an isoform of GRIN1 by PKC. Dephosphorylated on Ser-897 probably by protein phosphatase 2A (PPP2CB). Its phosphorylated state is influenced by the formation of the NMDAR-PPP2CB complex and the NMDAR channel activity. {ECO:0000250|UniProtKB:Q05586}.; PTM: Ubiquitinated via 'Lys-48'-linked ubiquitin chains by the E3 ubiquitin ligase complex, at least composed of CUL3, KCTD13 and RBX1; leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q05586}.
uniprot
proteins
protein_family
Glutamate-gated ion channel (TC 1.A.10.1) family
uniprot
proteins
protein_family
NR1/GRIN1 subfamily
uniprot
proteins
pubmed
12008020
uniprot
proteins
pubmed
12860921
uniprot
proteins
pubmed
14602821
uniprot
proteins
pubmed
1532151
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18849881
uniprot
proteins
pubmed
18940194
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19751394
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23524343
uniprot
proteins
pubmed
26041915
uniprot
proteins
pubmed
36058615
uniprot
proteins
pubmed
37142655
uniprot
proteins
pubmed
7790891
uniprot
proteins
pubmed
8060614
uniprot
proteins
pubmed
9049108
uniprot
proteins
sequence_length
938
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12008020, ECO:0000269|PubMed:1532151, ECO:0000269|PubMed:37142655, ECO:0000269|PubMed:8060614}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P35439}. Postsynaptic cell membrane {ECO:0000269|PubMed:36058615}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P35439}. Synaptic cell membrane {ECO:0000269|PubMed:26041915, ECO:0000269|PubMed:36058615}. Note=Synaptic cell membrane targeting is dependent of GRIN2B/GluN2B subunit (PubMed:26041915). Association with GRIN3A occurs in the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P35439, ECO:0000269|PubMed:26041915}.
uniprot
proteins
transmembrane_region
TRANSMEM 560..580; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P35439"; TRANSMEM 631..647; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P35439"; TRANSMEM 813..833; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P35439
uniprot
proteins