+ |
PRKCA |
phosphorylation
|
APLP2 |
0.346 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248970 |
Thr723 |
LRKRQYGtISHGIVE |
in vitro |
|
pmid |
sentence |
9109675 |
We report here that a cytoplasmic domain peptide from APLP1 is phosphorylated in vitro by protein kinase C and that a cytoplasmic domain peptide from APLP2 is phosphorylated in vitro by protein kinase C and cdc2 kinase. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
MAPK8 | up-regulates
phosphorylation
|
APLP2 |
0.37 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-122196 |
Thr736 |
VEVDPMLtPEERHLN |
Homo sapiens |
|
pmid |
sentence |
14970211 |
Phosphorylation at the thr(668) residue of app (with respect to the numbering conversion for the app 695 isoform) and the thr(736) residue of aplp2 (with respect to the numbering conversion for the aplp2 763 isoform) in their cytoplasmic domains acts as a molecular switch for their protein-protein interaction and is implicated in neural function(s) and/or alzheimer's disease pathogenesis. Here we demonstrate that both app and aplp2 can be phosphorylated by jnk at the thr(668) and thr(736) residues, respectively, in response to cellular stress. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK1 |
phosphorylation
|
APLP2 |
0.338 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-47483 |
Thr736 |
VEVDPMLtPEERHLN |
Homo sapiens |
|
pmid |
sentence |
9109675 |
A cytoplasmic domain peptide from aplp2 is phosphorylated in vitro by protein kinase c and cdc2 kinase. Aplp2 is phosphorylated by cdc2 kinase at a site homologous to the cdc2 kinase site phosphorylated in app. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Brain |