| + |
MAPK3 |
phosphorylation
|
APBB1 |
0.271 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120467 |
Ser175 |
EEEEDLSsPPGLPEP |
Homo sapiens |
|
| pmid |
sentence |
| 14697653 |
Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120475 |
Ser287 |
WEPPGRAsPSQGSSP |
Homo sapiens |
|
| pmid |
sentence |
| 14697653 |
Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120479 |
Ser347 |
TFPAQSLsPEPLPQE |
Homo sapiens |
|
| pmid |
sentence |
| 14697653 |
Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120483 |
Thr709 |
PKRLGAHtP |
Homo sapiens |
|
| pmid |
sentence |
| 14697653 |
Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
MAPK1 |
phosphorylation
|
APBB1 |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120451 |
Ser175 |
EEEEDLSsPPGLPEP |
Homo sapiens |
|
| pmid |
sentence |
| 14697653 |
Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120455 |
Ser287 |
WEPPGRAsPSQGSSP |
Homo sapiens |
|
| pmid |
sentence |
| 14697653 |
Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120459 |
Ser347 |
TFPAQSLsPEPLPQE |
Homo sapiens |
|
| pmid |
sentence |
| 14697653 |
Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120463 |
Thr709 |
PKRLGAHtP |
Homo sapiens |
|
| pmid |
sentence |
| 14697653 |
Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
ABL1 | up-regulates 
phosphorylation
|
APBB1 |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123476 |
Tyr547 |
VQKFQVYyLGNVPVA |
Homo sapiens |
|
| pmid |
sentence |
| 15031292 |
The c-abl tyrosine kinase phosphorylates the fe65 adaptor protein to stimulate fe65/amyloid precursor protein nuclear signaling. Here, we show that active c-abl stimulates app/fe65-mediated gene transcription and that this effect is mediated by phosphorylation of fe65 on tyrosine 547 within its second ptb domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APBB1 | up-regulates activity
relocalization
|
TSHZ3 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264813 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19343227 |
We carried out yeast two-hybrid studies with a PTB domain of FE65, focusing on those genes that might be involved in nuclear signaling, and identified and validated Teashirt proteins as FE65 interacting proteins in neurons. Using reporter systems, we observed that FE65 could simultaneously recruit SET, a component of the inhibitor of acetyl transferase, and Teashirt, which in turn recruited histone deacetylases, to produce a powerful gene-silencing complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta |
phosphorylation
|
APBB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270054 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14697653 |
Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 |
phosphorylation
|
APBB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270166 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14697653 |
Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
APBB1
- 
- 