| + |
CDK5 | up-regulates activity 
phosphorylation
|
GRIN2A |
0.541 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250666 |
Ser1232 |
SGHFTMRsPFKCDAC |
Rattus norvegicus |
Neuron |
| pmid |
sentence |
| 11675505 |
Here, we demonstrate that cyclin dependent kinase-5 (Cdk5) associates with and phosphorylates NR2A subunits at Ser-1232 in vitro and in intact cells. Moreover, we show that roscovitine, a selective Cdk5 inhibitor, blocks both long-term potentiation induction and NMDA-evoked currents in rat CA1 hippocampal neurons. These results suggest that Cdk5 plays a key role in synaptic transmission and plasticity through its up-regulation of NMDARs. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKCA |
phosphorylation
|
GRIN2A |
0.52 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249065 |
Ser1416 |
ASYCSRDsRGHNDVY |
Rattus norvegicus |
|
| pmid |
sentence |
| 11104776 |
PKC-dependent phosphorylation of NR2A(Ser(1416)) as a key mechanism in inhibiting alphaCaMKII-binding and promoting dissociation of alphaCaMKII.NR2A complex. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
SRC | up-regulates activity
phosphorylation
|
GRIN2A |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247163 |
Tyr1105 |
CSEVERTyLKTKSSS |
in vitro |
|
| pmid |
sentence |
| 10195142 |
To gain further insight into the roles of Src and Fyn in the phosphorylation and regulation of the NMDA receptor, we have characterized the tyrosine phosphorylation of NR2A and NR2B by exogenous Src and FynIn the case of NR2A, three potential tyrosine phosphorylation sites have been proposed: Tyr1105, Tyr1267 and Tyr1387 (Zheng et al. 1998; Bi et al. 2000), all of which are similarly located in the C-terminal, cytoplasmic domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247167 |
Tyr1267 |
PATGEQVyQQDWAQN |
in vitro |
|
| pmid |
sentence |
| 10195142 |
To gain further insight into the roles of Src and Fyn in the phosphorylation and regulation of the NMDA receptor, we have characterized the tyrosine phosphorylation of NR2A and NR2B by exogenous Src and FynIn the case of NR2A, three potential tyrosine phosphorylation sites have been proposed: Tyr1105, Tyr1267 and Tyr1387 (Zheng et al. 1998; Bi et al. 2000), all of which are similarly located in the C-terminal, cytoplasmic domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247171 |
Tyr1387 |
GRCPSDPyKHSLPSQ |
in vitro |
|
| pmid |
sentence |
| 10195142 |
To gain further insight into the roles of Src and Fyn in the phosphorylation and regulation of the NMDA receptor, we have characterized the tyrosine phosphorylation of NR2A and NR2B by exogenous Src and FynIn the case of NR2A, three potential tyrosine phosphorylation sites have been proposed: Tyr1105, Tyr1267 and Tyr1387 (Zheng et al. 1998; Bi et al. 2000), all of which are similarly located in the C-terminal, cytoplasmic domain. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
FYN | up-regulates activity
phosphorylation
|
GRIN2A |
0.724 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247151 |
Tyr1105 |
CSEVERTyLKTKSSS |
in vitro |
|
| pmid |
sentence |
| 10195142 |
To gain further insight into the roles of Src and Fyn in the phosphorylation and regulation of the NMDA receptor, we have characterized the tyrosine phosphorylation of NR2A and NR2B by exogenous Src and FynIn the case of NR2A, three potential tyrosine phosphorylation sites have been proposed: Tyr1105, Tyr1267 and Tyr1387 (Zheng et al. 1998; Bi et al. 2000), all of which are similarly located in the C-terminal, cytoplasmic domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247155 |
Tyr1267 |
PATGEQVyQQDWAQN |
in vitro |
|
| pmid |
sentence |
| 10195142 |
To gain further insight into the roles of Src and Fyn in the phosphorylation and regulation of the NMDA receptor, we have characterized the tyrosine phosphorylation of NR2A and NR2B by exogenous Src and FynIn the case of NR2A, three potential tyrosine phosphorylation sites have been proposed: Tyr1105, Tyr1267 and Tyr1387 (Zheng et al. 1998; Bi et al. 2000), all of which are similarly located in the C-terminal, cytoplasmic domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247159 |
Tyr1387 |
GRCPSDPyKHSLPSQ |
in vitro |
|
| pmid |
sentence |
| 10195142 |
To gain further insight into the roles of Src and Fyn in the phosphorylation and regulation of the NMDA receptor, we have characterized the tyrosine phosphorylation of NR2A and NR2B by exogenous Src and FynIn the case of NR2A, three potential tyrosine phosphorylation sites have been proposed: Tyr1105, Tyr1267 and Tyr1387 (Zheng et al. 1998; Bi et al. 2000), all of which are similarly located in the C-terminal, cytoplasmic domain. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
FYN | up-regulates
phosphorylation
|
GRIN2A |
0.724 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188527 |
Tyr1325 |
RLLEGNFyGSLFSVP |
Homo sapiens |
|
| pmid |
sentence |
| 19834457 |
The nr2a subunit of the nmda receptor is tyrosine-phosphorylated, with tyr 1325 as its one of the major phosphorylation site. Tyr 1325 phosphorylation site is required for src-induced potentiation of the nmda receptor channel in the striatum. Tyr 1325 was most prominently phosphorylated by fyn in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates
phosphorylation
|
GRIN2A |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188531 |
Tyr1325 |
RLLEGNFyGSLFSVP |
Homo sapiens |
|
| pmid |
sentence |
| 19834457 |
The nr2a subunit of the nmda receptor is tyrosine-phosphorylated, with tyr 1325 as its one of the major phosphorylation sitewe also show that the tyr 1325 phosphorylation site is required for src-induced potentiation of the nmda receptor channel in the striatum. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GRIN2A | form complex 
binding
|
NMDA receptor_2A |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264121 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 12871085 |
The NMDA receptor, a ligand-gated ion channel composed of the NR1 and NR2 subunits, is located mainly at synapses of CNS neurons. The NMDA receptor subtypes are encoded by three gene families that process mRNA transcripts to yield six distinct subunits (NR1, NR2A-2D, NR3A). Receptors are thought to be tetrameric complexes of two NR1 and two NR2 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GRIN2A | up-regulates quantity
relocalization
|
calcium(2+) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251578 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20950656 |
In addition, neurons also possess unique systems for local Ca2+ signaling at synapses including; presynaptic voltage-gated Ca2+ channels coupled to the synaptic vesicle membrane fusion machinery [39]; postsynaptic excitatory glutamate receptor channels which flux either Na+ (AMPA receptors) or Ca2+ (NMDA receptors) [40] and [41]; and Ca2+-binding proteins |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN5 | down-regulates activity 
dephosphorylation
|
GRIN2A |
0.443 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277089 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27857196 |
STEP inhibition by TC-2153 enhanced Tyr phosphorylation of GluN2A (XREF_FIG, 1 EGTA+TC-2153, n = 5, P < 0.05 compared with 1mM EGTA) without altering phosphorylation of Src (XREF_FIG, 1 EGTA+TC-2153, n = 5, P> 0.05 compared with 1 EGTA).|These findings confirm that not only GluN2B and Fyn but also GluN2A are substrates of STEP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLG4 | up-regulates activity
relocalization
|
GRIN2A |
0.804 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264194 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 9278515 |
The PDZ domains of PSD-95 and related proteins interact with the COOH-terminal sequences of K+channels and NMDA2 receptors (3). By these interactions, PSD-95 may mediate the clustering of K+ channels and NMDA receptors at synapses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
GRIN2A
- 
- 