| + |
CAMK2G | up-regulates activity 
phosphorylation
|
GRIA1 |
0.61 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250697 |
Ser645 |
LTVERMVsPIESAED |
|
HEK-293 Cell |
| pmid |
sentence |
| 7877986 |
In this study, CaM-kinase II enhanced kainate currents of expressed glutamate receptor 6 in 293 cells and of wild-type glutamate receptor 1, but not the Ser-627 to Ala mutant, in Xenopus oocytes. | This CaM-kinase II regulatory phosphorylation site is conserved in all AMPA/kainate-type glutamate receptors, and its phosphorylation may be important in enhancing postsynaptic responsiveness as occurs during synaptic plasticity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250698 |
Ser849 |
FCLIPQQsINEAIRT |
|
|
| pmid |
sentence |
| 12609872 |
Direct phosphorylation of the GluR1 subunit of postsynaptic AMPA receptors by Ca(2+)/calmodulin-dependent protein kinase II (CaM-KII) is believed to be one of the major contributors to the enhanced strength of glutamatergic synapses in CA1 area of hippocampus during long-term potentiation. | Validity of the approach was confirmed by modeling, and silence analysis was applied then to the GluR1 AMPA receptor mutated at S831, the site phosphorylated by CaM-KII during long-term potentiation. Silence analysis indicates that a negative charge at S831 is a critical determinant for the enhanced channel function as a charge carrier. Silence and variance analyses, when applied to the same sets of data, were in agreement on the receptor regulation upon mutations. |
|
| Publications: |
2 |
| + |
PRKCA |
phosphorylation
|
GRIA1 |
0.703 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248950 |
Ser832 |
LIEFCYKsRSESKRM |
Homo sapiens |
|
| pmid |
sentence |
| 8663994 |
In addition, protein kinase C specifically phosphorylates Ser-831 of GluR1 in HEK-293 cells and in cultured neurons. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates activity
phosphorylation
|
GRIA1 |
0.469 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249987 |
Ser863 |
TSTLPRNsGAGASSG |
Homo sapiens |
|
| pmid |
sentence |
| 8663994 |
Phosphorylation of Ser-845 on GluR1 by PKA potentiates its response to glutamate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GRIA1 | up-regulates 
|
Excitatory_synaptic_transmission |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261433 |
|
|
Mus musculus |
Neuron |
| pmid |
sentence |
| 15115814 |
The targeting and clustering of AMPA and NMDA receptors to synapses in the CNS is essential for efficient excitatory synaptic transmission |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264615 |
|
|
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: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
IQSEC2 | up-regulates quantity
relocalization
|
GRIA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264912 |
|
|
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 |
| + |
NPTX1 | up-regulates activity
binding
|
GRIA1 |
0.304 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261430 |
|
|
Mus musculus |
Neuron |
| pmid |
sentence |
| 15115814 |
We found that NP1 colocalizes and physically associates with the fast excitatory GluR1 AMPA receptors and that hypoxia induces a time-dependent increase in the NP1-GluR1 interactions. Thus hypoxia recruits NP1 protein to GluR1 subunits concurrent with the hypoxic excitotoxic cascade.|Rather we propose that through interactions with GluR1 clusters, NP1 modulates the function of AMPA receptors in a manner whereby increased NP1-GluR1 interactions sensitize neurons to hypoxia-induced excitotoxic death. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
glutamic acid | up-regulates activity
chemical activation
|
GRIA1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261432 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 15115814 |
AMPA glutamate receptor subunit (GluR1) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264616 |
|
|
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: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
GRIA1 | up-regulates quantity
relocalization
|
calcium(2+) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264947 |
|
|
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 |
| + |
SHANK3 | up-regulates quantity
binding
|
GRIA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264601 |
|
|
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 |
3.0
GRIA1
- 
- 