| + |
PRKCA |
phosphorylation
|
GRIA2 |
0.698 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248954 |
Ser683 |
TKEFFRRsKIAVFDK |
in vitro |
|
| pmid |
sentence |
| 8848293 |
Only two peptides containing Ser-662 and Ser-696 were found to be efficiently phosphorylated by protein kinase C (PKC). The peptide including Ser-696 was also phosphorylated by protein kinase G (PKG). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248955 |
Ser717 |
GVARVRKsKGKYAYL |
in vitro |
|
| pmid |
sentence |
| 8848293 |
Only two peptides containing Ser-662 and Ser-696 were found to be efficiently phosphorylated by protein kinase C (PKC). The peptide including Ser-696 was also phosphorylated by protein kinase G (PKG). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249022 |
Ser880 |
YNVYGIEsVKI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10501226 |
Here, we show that the C terminus of GluR2 of the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptor is phosphorylated by protein kinase C and that serine-880 is the major phosphorylation site. This phosphorylation also occurs in human embryonic kidney (HEK) cells by addition of 12-O-tetradecanoylphorbol 13-acetate. |
|
| Publications: |
3 |
Organism: |
In Vitro, Homo Sapiens |
| + |
glutamic acid | up-regulates activity 
chemical activation
|
GRIA2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264609 |
|
|
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 |
| + |
GRIA2 | up-regulates 
|
Excitatory_synaptic_transmission |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264612 |
|
|
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 |
| + |
PICK1 | up-regulates activity
binding
|
GRIA2 |
0.801 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264046 |
|
|
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 |
| + |
MECP2 | down-regulates quantity by repression 
transcriptional regulation
|
GRIA2 |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264684 |
|
|
Rattus norvegicus |
|
| 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 |
| Pathways: | Rett syndrome |
| + |
GRIA2 | up-regulates
|
Synaptic_plasticity |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265796 |
|
|
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: |
1 |
Organism: |
In Vitro |
| Pathways: | Rett syndrome |
| + |
PTPN5 | down-regulates activity
dephosphorylation
|
GRIA2 |
0.423 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277040 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21883219 |
One study showed that stimulation of the metabotrophic glutamate receptor mGluR5 leads to a STEP mediated tyrosine dephosphorylation of GluA2 and internalization of GluA1 and GluA2, although the tyrosine residue on GluA2 that is dephosphorylated by STEP remains unidentified. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IQSEC2 | up-regulates quantity
relocalization
|
GRIA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264913 |
|
|
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 |
| + |
GRIA2 | up-regulates quantity
relocalization
|
calcium(2+) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264948 |
|
|
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
|
GRIA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264602 |
|
|
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
GRIA2
- 
- 