| + |
PRKCA | up-regulates activity 
phosphorylation
|
GRIN2B |
0.486 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249083 |
Ser1303 |
NKLRRQHsYDTFVDL |
in vitro |
|
| pmid |
sentence |
| 11306676 |
These results indicate that PKC can directly phosphorylate S1303 and S1323 in the NR2B C terminus, leading to enhanced currents through NMDA receptor channels. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249086 |
Ser1323 |
ALAPRSVsLKDKGRF |
in vitro |
|
| pmid |
sentence |
| 11306676 |
These results indicate that PKC can directly phosphorylate S1303 and S1323 in the NR2B C terminus, leading to enhanced currents through NMDA receptor channels. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCB | up-regulates activity
phosphorylation
|
GRIN2B |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249084 |
Ser1303 |
NKLRRQHsYDTFVDL |
in vitro |
|
| pmid |
sentence |
| 11306676 |
These results indicate that PKC can directly phosphorylate S1303 and S1323 in the NR2B C terminus, leading to enhanced currents through NMDA receptor channels. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249087 |
Ser1323 |
ALAPRSVsLKDKGRF |
in vitro |
|
| pmid |
sentence |
| 11306676 |
These results indicate that PKC can directly phosphorylate S1303 and S1323 in the NR2B C terminus, leading to enhanced currents through NMDA receptor channels. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CAMK2A | up-regulates activity
phosphorylation
|
GRIN2B |
0.684 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250630 |
Ser1303 |
NKLRRQHsYDTFVDL |
|
Hippocampal Cell Line |
| pmid |
sentence |
| 8940188 |
By peptide mapping, automated sequencing, and mass spectrometry, we identified the major site of phosphorylation on the fusion protein as Ser-383, corresponding to Ser-1303 of full-length NR2B. The Km for phosphorylation of this site in the fusion protein was approximately 50 nM, much lower than that of other known substrates for CaM kinase II, suggesting that the receptor is a high affinity substrate. We show that serine 1303 in the full-length NR2B and/or the cognate site in NR2A is a major site of phosphorylation of the receptor both in the postsynaptic density fraction and in living hippocampal neurons. |
|
| Publications: |
1 |
| + |
PRKCG | up-regulates activity
phosphorylation
|
GRIN2B |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249085 |
Ser1303 |
NKLRRQHsYDTFVDL |
in vitro |
|
| pmid |
sentence |
| 11306676 |
These results indicate that PKC can directly phosphorylate S1303 and S1323 in the NR2B C terminus, leading to enhanced currents through NMDA receptor channels. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249088 |
Ser1323 |
ALAPRSVsLKDKGRF |
in vitro |
|
| pmid |
sentence |
| 11306676 |
These results indicate that PKC can directly phosphorylate S1303 and S1323 in the NR2B C terminus, leading to enhanced currents through NMDA receptor channels. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CAMK2B | up-regulates activity
phosphorylation
|
GRIN2B |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250688 |
Ser1303 |
NKLRRQHsYDTFVDL |
|
Hippocampal Cell Line |
| pmid |
sentence |
| 8940188 |
By peptide mapping, automated sequencing, and mass spectrometry, we identified the major site of phosphorylation on the fusion protein as Ser-383, corresponding to Ser-1303 of full-length NR2B. The Km for phosphorylation of this site in the fusion protein was approximately 50 nM, much lower than that of other known substrates for CaM kinase II, suggesting that the receptor is a high affinity substrate. We show that serine 1303 in the full-length NR2B and/or the cognate site in NR2A is a major site of phosphorylation of the receptor both in the postsynaptic density fraction and in living hippocampal neurons. |
|
| Publications: |
1 |
| + |
CSNK2A1 | down-regulates 
phosphorylation
|
GRIN2B |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-130336 |
Ser1479 |
HVYEKLSsIESDV |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15537897 |
Here we show that casein kinase ii (ck2) phosphorylates the serine residue (ser1480) within the c-terminal pdz ligand (iesdv) of the nr2b subunit of nmdar in vitro and in vivo. Phosphorylation of ser1480 disrupts the interaction of nr2b with the pdz domains of psd-95 and sap102 and decreases surface nr2b expression in neurons. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FYN |
phosphorylation
|
GRIN2B |
0.761 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251169 |
Tyr1039 |
HSQLSDLyGKFSFKS |
in vitro |
|
| pmid |
sentence |
| 11024032 |
Tyr-932, Tyr-1039, Tyr-1070, Tyr-1109, Tyr-1252, Tyr-1336, and Tyr-1472 are Fyn-mediated phosphorylation sites in GluRε2 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251170 |
Tyr1070 |
ISTHTVTyGNIEGNA |
in vitro |
|
| pmid |
sentence |
| 11024032 |
Tyr-932, Tyr-1039, Tyr-1070, Tyr-1109, Tyr-1252, Tyr-1336, and Tyr-1472 are Fyn-mediated phosphorylation sites in GluRε2 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251171 |
Tyr1109 |
FDEIELAyRRRPPRS |
in vitro |
|
| pmid |
sentence |
| 11024032 |
Tyr-932, Tyr-1039, Tyr-1070, Tyr-1109, Tyr-1252, Tyr-1336, and Tyr-1472 are Fyn-mediated phosphorylation sites in GluRε2 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251172 |
Tyr1252 |
CKKAGNLyDISEDNS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11024032 |
Tyr-1252, Tyr-1336, and Tyr-1472 of GluRε2 are phosphorylated in 293T cells when active Fyn is co-expressed. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251173 |
Tyr1336 |
RFMDGSPyAHMFEMS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11024032 |
Tyr-1252, Tyr-1336, and Tyr-1472 of GluRε2 are phosphorylated in 293T cells when active Fyn is co-expressed. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249338 |
Tyr1474 |
GSSNGHVyEKLSSIE |
|
|
| pmid |
sentence |
| 11483655 |
We have investigated the tyrosine phosphorylation of NMDA receptor subunits NR2A and NR2B by exogenous Src and Fyn and compared this to phosphorylation by tyrosine kinases associated with the postsynaptic density (PSD)|Phosphorylation-site specific antibodies identified NR2B Tyr1472 as a phosphorylation site for intrinsic PSD tyrosine kinases |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251175 |
Tyr1474 |
GSSNGHVyEKLSSIE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11024032 |
Tyr-1252, Tyr-1336, and Tyr-1472 of GluRε2 are phosphorylated in 293T cells when active Fyn is co-expressed. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251174 |
Tyr932 |
IRRESSVyDISEHRR |
in vitro |
|
| pmid |
sentence |
| 11024032 |
Tyr-932, Tyr-1039, Tyr-1070, Tyr-1109, Tyr-1252, Tyr-1336, and Tyr-1472 are Fyn-mediated phosphorylation sites in GluRε2 in vitro. |
|
| Publications: |
8 |
Organism: |
In Vitro, Homo Sapiens, |
| + |
FYN | up-regulates activity
phosphorylation
|
GRIN2B |
0.761 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247176 |
Tyr1474 |
GSSNGHVyEKLSSIE |
in vitro |
|
| pmid |
sentence |
| 11483655 |
We have investigated the tyrosine phosphorylation of NMDA receptor subunits NR2A and NR2B by exogenous Src Phosphorylation-site specific antibodies identified NR2B Tyr1472 as a phosphorylation site for intrinsic PSD tyrosine kinases |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PTPRG | up-regulates activity
dephosphorylation
|
GRIN2B |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254702 |
Tyr1474 |
GSSNGHVyEKLSSIE |
in vitro |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SRC | up-regulates activity
phosphorylation
|
GRIN2B |
0.583 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247180 |
Tyr1474 |
GSSNGHVyEKLSSIE |
in vitro |
|
| pmid |
sentence |
| 11483655 |
We have investigated the tyrosine phosphorylation of NMDA receptor subunits NR2A and NR2B by exogenous Src Phosphorylation-site specific antibodies identified NR2B Tyr1472 as a phosphorylation site for intrinsic PSD tyrosine kinases |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PTPN5 | down-regulates activity
dephosphorylation
|
GRIN2B |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265744 |
Tyr1474 |
GSSNGHVyEKLSSIE |
Mus musculus |
Cerebral Cortical Neuron |
| pmid |
sentence |
| 20427654 |
These previous results, together with the present findings, indicate that STEP61 dephosphorylates the NR2B subunit at its regulatory tyr1472 site, and dephosphorylation of this site leads to internalization of the NMDAR complex from neuronal surface membranes. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
GRIN2B | form complex 
binding
|
NMDA receptor_2B |
0.71 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264123 |
|
|
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 |
| + |
MECP2 | down-regulates quantity by repression
transcriptional regulation
|
GRIN2B |
0.363 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264685 |
|
|
Rattus norvegicus |
Cerebral Cortical Neuron |
| pmid |
sentence |
| 18952054 |
The interaction of MeCP2 with the 2BI3 and 2BI5 sites was strikingly reduced in neurons maintained in the presence of TTX (Fig. 2C). This result is consistent with the classical view of MeCP2 as a general transcriptional repressor, in that the reduced association leads to increased expression of NR2B. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
DLG4 | up-regulates activity
relocalization
|
GRIN2B |
0.818 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264195 |
|
|
Homo sapiens |
|
| 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 |
| + |
FOXP2 | up-regulates quantity by expression
transcriptional regulation
|
GRIN2B |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266834 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25232744 |
By interacting with CASK, TBR1 regulates several ASD candidate genes, such as GRIN2B, AUTS2 and RELN—all of which are recurrently mutated in ASD. In areas of the brain with overlapping expression patterns, such as in glutamatergic layer 6 neurons, the TBR1–FOXP2 interaction may result in co-ordinated regulation of common downstream targets. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
3.0
GRIN2B
- 
- 