+ |
PRKCA | up-regulates
phosphorylation
|
GRIA4 |
0.551 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97554 |
Ser862 |
IRNKARLsITGSVGE |
Homo sapiens |
|
pmid |
sentence |
12536214 |
Receptor internalization, altered;intracellular localization |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CAMK2A | up-regulates
phosphorylation
|
GRIA4 |
0.574 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97546 |
Ser862 |
IRNKARLsITGSVGE |
Homo sapiens |
|
pmid |
sentence |
12536214 |
Receptor internalization, altered;intracellular localization |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKACA | up-regulates
phosphorylation
|
GRIA4 |
0.415 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97550 |
Ser862 |
IRNKARLsITGSVGE |
Homo sapiens |
|
pmid |
sentence |
12536214 |
We found that pka phosphorylation of the ampa receptor subunits glur4 and glur1 directly controlled the synaptic incorporation of ampa receptors in organotypic slices from rat hippocampus. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCG | up-regulates
phosphorylation
|
GRIA4 |
0.691 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97558 |
Ser862 |
IRNKARLsITGSVGE |
Homo sapiens |
|
pmid |
sentence |
12536214 |
We found that pka phosphorylation of the ampa receptor subunits glur4 and glur1 directly controlled the synaptic incorporation of ampa receptors in organotypic slices from rat hippocampus. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CAMK2G |
phosphorylation
|
GRIA4 |
0.507 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250699 |
Ser862 |
IRNKARLsITGSVGE |
|
|
pmid |
sentence |
10366608 |
We found that GluR4 is phosphorylated on serine 842 within the C-terminal domain in vitro and in vivo. Serine 842 is phosphorylated by PKA, PKC, and CaMKII in vitro and is phosphorylated in transfected cells by PKA. |
|
Publications: |
1 |
+ |
PRKCA |
phosphorylation
|
GRIA4 |
0.551 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249017 |
Thr850 |
EAKRMKLtFSEAIRN |
in vitro |
|
pmid |
sentence |
10366608 |
In addition, we identified threonine 830 as a potential PKC phosphorylation site. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
FUS | down-regulates quantity by repression
post transcriptional regulation
|
GRIA4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262806 |
|
|
Mus musculus |
|
pmid |
sentence |
28515487 |
This conclusion is also supported by the analysis of alternative splicing events in hFUS+/+; Smn+/− mice. As shown in Fig. 6b, the splicing of Dusp22, Mphosph9, Adarb1, hnRNP A2/B1, Gria4, Vps16, Atxn2 and Agrin, which are significantly affected in hFUS+/+ mice, is not further modified by SMN decrease |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Spinal Cord |
+ |
SHANK3 | up-regulates quantity
binding
|
GRIA4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264604 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
28179641 |
SHANK proteins are ‘master’ scaffolding proteins that tether and organize intermediate scaffolding proteins. They are located at excitatory synapses, where they are crucial for proper synaptic development and function. SAPAP proteins subsequently bind to the PDZ domain of members of the SHANK protein family. SHANK proteins then bind to the actin cytoskeleton and to Homer protein, which in turn interacts with mGluRs. Through these extended links, PSD95, SAPAP, SHANK and Homer proteins form a quaternary complex that brings together mGluR and NMDAR complexes in the PSD (FIG. 3). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
glutamic acid | up-regulates activity
chemical activation
|
GRIA4 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264611 |
|
|
Homo sapiens |
|
pmid |
sentence |
30825796 |
In the mammalian brain the majority of fast excitatory neurotransmission is carried out by α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive ionotropic glutamate receptors located within the post-synaptic density of glutamatergic synapses |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IQSEC2 | up-regulates quantity
relocalization
|
GRIA4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264915 |
|
|
Homo sapiens |
|
pmid |
sentence |
27009485 |
BRAG1 increases the synaptic recycling pool of AMPARs.these data suggest that the BRAG1 enhancement of AMPAR transmission is mediated by the increased expression of the recycling pool of synaptic GluA2/3 receptors. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Brain |
+ |
GRIA4 | up-regulates
|
Excitatory_synaptic_transmission |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264614 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
30825796 |
In the mammalian brain the majority of fast excitatory neurotransmission is carried out by α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive ionotropic glutamate receptors located within the post-synaptic density of glutamatergic synapses |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GRIA4 | up-regulates quantity
relocalization
|
calcium(2+) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264950 |
|
|
Homo sapiens |
|
pmid |
sentence |
29953871 |
Ca2+ is arguably the most important second messenger in the brain because of its pivotal roles in presynaptic neurotransmitter release, postsynaptic responses, and plasticity induction. iGluRs and mGluRs can generate intracellular Ca2+ signals, albeit by different mechanisms, whose crosstalk has not been thoroughly explored (Figure 2C). iGluRs allow the influx of extracellular Ca2+ upon pore opening. This is widely acknowledged for NMDARs, which have a high Ca2+ conductance, but Ca2+ flux through AMPARs and KARs can still be substantial. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |