| + |
CAMK2A | up-regulates 
phosphorylation
|
AMPA |
0.643 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270230 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12536214 |
Receptor internalization, altered;intracellular localization |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamatergic synapse |
| + |
AMPA | up-regulates 
|
Synaptic_plasticity |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270304 |
|
|
in vitro |
|
| pmid |
sentence |
| 32527803 |
AMPAR surface diffusion tunes short-term plasticity. | Accordingly, recent studies have suggested that about half of synaptic AMPARs are organized in nanoclusters that are aligned with presynaptic transmitter release sites, supporting the concept of functional nanocolumns to increase the fidelity of fast excitatory transmission. This peculiar organization might also support the proposal that we made 10 years ago that fast surface diffusion of AMPARs tunes frequency-dependent short-term plasticity (FD-STP) by allowing the fast replacement of desensitized receptors by naïve ones. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267783 |
|
|
in vitro |
|
| pmid |
sentence |
| 32527803 |
AMPAR surface diffusion tunes short-term plasticity. | Accordingly, recent studies have suggested that about half of synaptic AMPARs are organized in nanoclusters that are aligned with presynaptic transmitter release sites, supporting the concept of functional nanocolumns to increase the fidelity of fast excitatory transmission. This peculiar organization might also support the proposal that we made 10 years ago that fast surface diffusion of AMPARs tunes frequency-dependent short-term plasticity (FD-STP) by allowing the fast replacement of desensitized receptors by naïve ones. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | Dopaminergic Synapse, Glutamatergic synapse |
| + |
glutamic acid | up-regulates activity
chemical activation
|
AMPA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264696 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15919192 |
Glutamate receptor ion channels mediate excitatory responses at the majority of CNS synapses. The glutamate receptor ion channels (iGluRs) are abundantly expressed in the brain and spinal cord and mediate responses at the vast majority of excitatory synapses. Mammalian iGluRs are encoded by 18 genes that assemble to form four major families, the AMPA, kainate, NMDA and delta receptors. There are four AMPA receptor genes (GluR1–4); five kainate receptor genes (GluR5–7, plus KA1 and KA2); seven NMDA receptor genes (NR1, NR2A-D, NR3A and NR3B); and two delta subunits. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Dopaminergic Synapse, Glutamatergic synapse |
| + |
SHANK3 | up-regulates quantity
relocalization
|
AMPA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264700 |
|
|
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 |
| Pathways: | Glutamatergic synapse |
| + |
NPTX1 | up-regulates activity
binding
|
AMPA |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270235 |
|
|
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 |
| + |
PRKACA | up-regulates activity
phosphorylation
|
AMPA |
0.487 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267784 |
|
YES |
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 |
| + |
IQSEC2 | up-regulates quantity
relocalization
|
AMPA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264916 |
|
|
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 |
| + |
CAMK2G | up-regulates activity
phosphorylation
|
AMPA |
0.614 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270234 |
|
|
|
|
| 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: |
1 |
| + |
AMPA | up-regulates quantity
relocalization
|
calcium(2+) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264941 |
|
|
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 |
| Pathways: | Dopaminergic Synapse, Glutamatergic synapse |
| + |
AMPA | up-regulates
|
Excitatory_synaptic_transmission |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264695 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15919192 |
Glutamate receptor ion channels mediate excitatory responses at the majority of CNS synapses. The glutamate receptor ion channels (iGluRs) are abundantly expressed in the brain and spinal cord and mediate responses at the vast majority of excitatory synapses. Mammalian iGluRs are encoded by 18 genes that assemble to form four major families, the AMPA, kainate, NMDA and delta receptors. There are four AMPA receptor genes (GluR1–4); five kainate receptor genes (GluR5–7, plus KA1 and KA2); seven NMDA receptor genes (NR1, NR2A-D, NR3A and NR3B); and two delta subunits. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Dopaminergic Synapse, Glutamatergic synapse |
| + |
PRKCG | up-regulates
phosphorylation
|
AMPA |
0.693 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270233 |
|
|
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 |
| + |
MECP2 | down-regulates quantity by repression 
transcriptional regulation
|
AMPA |
0.332 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270237 |
|
|
Rattus norvegicus |
Cerebral Cortical Neuron |
| pmid |
sentence |
| 22262897 |
Bicuculline treatment also leads to an increase in the levels of the transcriptional repressor MeCP2, which binds to the GluR2 promoter along with the corepressors HDAC1 and mSin3A. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
FUS | down-regulates quantity by repression 
post transcriptional regulation
|
AMPA |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270231 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 28515487 |
This conclusion is also supported by the analysis of alternative splicing events inhFUS+/+;Smn+/‚àímice. As shown in Fig.6b, the splicing of Dusp22, Mphosph9, Adarb1, hnRNP A2/B1, Gria4, Vps16, Atxn2 and Agrin, which are significantly affected inhFUS+/+mice, is not further modified by SMN decrease |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Spinal Cord |
| + |
PPP1CA | down-regulates activity
dephosphorylation
|
AMPA |
0.504 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265060 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14751588 |
Dopamine and cyclic adenosine 3',5'-monophosphate-regulated phosphoprotein, 32 kDa (DARPP-32) is a key element of dopamine/D1/DARPP-32/protein phosphatase-1 (PP-1) signaling cascades of mammalian brain. Phosphorylation of AMPA receptors due to DARPP-32/PP1 signaling cascade increases AMPA channel activity and currents |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Dopaminergic Synapse |
| + |
PRKCA |
phosphorylation
|
AMPA |
0.704 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269853 |
|
|
in vitro |
|
| pmid |
sentence |
| 10366608 |
In addition, we identified threonine 830 as a potential PKC phosphorylation site. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKACA | up-regulates
phosphorylation
|
AMPA |
0.487 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270232 |
|
|
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 |
| + |
PICK1 | up-regulates activity
binding
|
AMPA |
0.801 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270236 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 25784538 |
RAB39B directs GluA2 trafficking in neurons. GTP-bound RAB39B interacts with PICK1. In line with evidence that PICK1 can dimerize, the structural model suggests that dimerization of PICK1 is a prerequisite for simultaneous recognition of both RAB39B and GluA2 each by one of the PICK1 molecules in the PICK1 dimer (Fig. 6a–c). The existence of such complex is supported by our co-immunoprecipitation experiments shown above. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
3.0
AMPA