| + |
ATG9A | up-regulates activity 
binding
|
YWHAE |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266368 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25266655 |
Our data suggest that the localization of mammalian Atg9A to autophagosomes requires phosphorylation on the C terminus of Atg9A at S761, which creates a 14-3-3ζ docking site. Under basal conditions, this phosphorylation is maintained at a low level and is dependent on both ULK1 and AMPK. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YWHAE | down-regulates 
binding
|
CDKN1B |
0.519 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88297 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12042314 |
14-3-3_, 14-3-3_, and 14-3-3_ (but not 14-3-3_ and 14-3-3_) could form a complex with p27kip1 / we discovered that akt-mediated p27kip1phosphorylation directly induces p27kip1binding to 14-3-3 and cytoplasmic localization through phosphorylating the newly identified thr198residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YWHAE | down-regulates activity
binding
|
NEFL |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252398 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23230147 |
These results suggest the important role of 14-3-3 in the dynamic regulation of NF-L assembly, and in the capacity to prevent the formation of NF-L aggregates. all seven isoforms specifically interacted with NF-L, but not NF-M or NF-H. specific interaction of 14-3-3 proteins with phosphorylated NF-L subunits also indicated the role of 14-3-3 and NF-L phosphorylation in the disassembly of neurofilaments. What is more, binding of 14-3-3 to phosphorylated NF-L subunits may prevent the dephosphorylation of these subunits by phosphatases, maintaining the hyperphosphorylation state of the subunits, which facilitates the disassembly of neurofilaments. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YWHAE | up-regulates activity
binding
|
TBP |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262834 |
|
|
|
|
| pmid |
sentence |
| 10449590 |
The in vitro binding with general transcription factors TBP and TFIIB together with its nuclear location provide evidence supporting a role for 14-3-3 proteins as transcriptional activators or coactivators when part of a DNA binding complex. |
|
| Publications: |
1 |
| + |
YWHAE | up-regulates activity
binding
|
NDEL1 |
0.652 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252160 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 17202468 |
14-3-3epsilon is involved in the proper localization of NUDEL and LIS1 in axons. 14-3-3ε binds to NUDEL phosphorylated by cyclin-dependent kinase (cdk5) and maintains NUDEL phosphorylation. Deficiency of 14-3-3ε causes mislocalization of the NUDEL/LIS1 complex from axons, suggesting that 14-3-3ε regulates the axonal targeting of the NUDEL/LIS1 complex by sustaining NUDEL phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YWHAE | up-regulates quantity by stabilization
binding
|
GRIN2C |
0.322 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262622 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 19477150 |
Here, we demonstrate that PKB/Akt directly phosphorylates NR2C on serine 1096 (S1096). In addition, we identify 14-3-3epsilon as an NR2C interactor, whose binding is dependent on S1096 phosphorylation. These data are all consistent with a model in which NR1 and NR2C oligomerize, PKB phosphorylates S1096, and 14-3-3ε binds to phosphorylated NR2C thereby promoting NR2C-containing NMDA receptor surface expression in cerebellar granule cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
YWHAE
- 
- 