GRIA2
entrez
2891
canonical
uniprot
P42262
canonical
ensembl
ENSG00000120251
resolver
ensp
ENSP00000264426
resolver
ensp
ENSP00000296526
resolver
ensp
ENSP00000377403
resolver
ensp
ENSP00000426845
resolver
ensp
ENSP00000515446
resolver
ensp
ENSP00000515463
resolver
enst
ENST00000703717
resolver
enst
ENST00000703754
resolver
genesymbol
GRIA2
resolver
genesymbol_syn
GLUR2
resolver
genesymbol_syn
GluA2
resolver
hgnc
HGNC:4572
resolver
uniprot
A0A994J4F1
resolver
uniprot
A8MT92
resolver
uniprot
I6L997
resolver
uniprot
Q96FP6
resolver
uniprot_entry
A0A994J4F1_HUMAN
resolver
uniprot_entry
GRIA2_HUMAN
resolver
uniprot_sec
A8MT92
resolver
uniprot_sec
I6L997
resolver
uniprot_sec
Q96FP6
resolver
amino_acid_sequence
MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDEMYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI
uniprot
proteins
disease_involvement
DISEASE: Neurodevelopmental disorder with language impairment and behavioral abnormalities (NEDLIB) [MIM:618917]: A neurodevelopmental disorder characterized by global developmental delay, impaired intellectual development, poor or absent speech, and behavioral abnormalities, such as autism spectrum disorder, repetitive behaviors, and hyperactivity. Some patients develop seizures and manifest developmental regression. {ECO:0000269|PubMed:31300657}. Note=The disease is caused by variants affecting the gene represented in this entry. The genetic variation producing the missense variant p.Q607E, associated with NEDLIB, is predicted to deeply affect RNA editing. In a physiological context, the adenosine (A) residue of the original glutamine (Q) codon CAG is post-transcriptionaly edited to inosine (I) by ADAR2, leading to a codon recognized by the ribosome as arginine (R). The glutamate (E) codon GAG, resulting from the genetic variation, is predicted to be edited 90% less than the normal CAG codon. If edited, the codon GIG would be translated as p.Q607G. {ECO:0000305|PubMed:31300657}.
uniprot
proteins
function
FUNCTION: Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid (PubMed:20614889, PubMed:31300657, PubMed:8003671). L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system and plays an important role in fast excitatory synaptic transmission (PubMed:14687553). Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse upon entry of monovalent and divalent cations such as sodium and calcium (PubMed:20614889, PubMed:8003671). The receptor then desensitizes rapidly and enters in a transient inactive state, characterized by the presence of bound agonist (By similarity). In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of L-glutamate (By similarity). Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity). {ECO:0000250|UniProtKB:P19491, ECO:0000269|PubMed:14687553, ECO:0000269|PubMed:20614889, ECO:0000269|PubMed:31300657, ECO:0000269|PubMed:8003671}.
uniprot
proteins
mass_dalton
98821
uniprot
proteins
post_translational_modification
PTM: Palmitoylated. Depalmitoylated upon L-glutamate stimulation. Cys-610 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-836 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis. {ECO:0000250|UniProtKB:P23819}.; PTM: Ubiquitinated by RNF167, leading to its degradation. {ECO:0000269|PubMed:23129617}.; PTM: Phosphorylation at Tyr-876 is required for interaction with IQSEC1 and ARF6 activation, which in turn triggers AMPAR internalization for persistent synaptic depression. {ECO:0000250|UniProtKB:P19491}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P23819}.
uniprot
proteins
protein_family
GRIA2 subfamily
uniprot
proteins
protein_family
Glutamate-gated ion channel (TC 1.A.10.1) family
uniprot
proteins
pubmed
14687553
uniprot
proteins
pubmed
15247289
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
19651138
uniprot
proteins
pubmed
20614889
uniprot
proteins
pubmed
21531559
uniprot
proteins
pubmed
23129617
uniprot
proteins
pubmed
23739980
uniprot
proteins
pubmed
31300657
uniprot
proteins
pubmed
7523595
uniprot
proteins
pubmed
8003671
uniprot
proteins
sequence_length
883
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23739980, ECO:0000269|PubMed:31300657}; Multi-pass membrane protein {ECO:0000269|PubMed:23739980}. Postsynaptic cell membrane {ECO:0000269|PubMed:23739980}; Multi-pass membrane protein {ECO:0000269|PubMed:23739980}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P23819}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23819}. Note=Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression (By similarity). Displays a somatodendritic localization and is excluded from axons in neurons (By similarity). {ECO:0000250|UniProtKB:P19491, ECO:0000250|UniProtKB:P23819}.
uniprot
proteins
transmembrane_region
TRANSMEM 544..564; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 617..637; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 813..833; /note="Helical; Name=M4
uniprot
proteins