+ |
SRPK2 | up-regulates activity
phosphorylation
|
LGMN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273569 |
Ser226 |
CYYDEKRsTYLGDWY |
Rattus norvegicus |
Neuron |
pmid |
sentence |
28826672 |
Here we report that serine-arginine protein kinase 2 (SRPK2) phosphorylates delta-secretase and enhances its enzymatic activity. SRPK2 phosphorylates serine 226 on delta-secretase and accelerates its autocatalytic cleavage, leading to its cytoplasmic translocation and escalated enzymatic activities. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
HSP90AA1 | up-regulates quantity by stabilization
binding
|
LGMN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272855 |
|
|
Homo sapiens |
MDA-MB-231 Cell |
pmid |
sentence |
24610907 |
We demonstrate that TRAF6 ubiquitinates the proform of AEP through K63-linked polyubiquitin, reversible by USP17, and forms a complex with HSP90α to subsequently promote pro-AEP intracellular stability as well as secretion. We now present evidence that AEP is a substrate for TRAF6 ubiquitination, resulting in AEP/TRAF6/HSP90α complex formation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
USP17L2 | down-regulates quantity by destabilization
deubiquitination
|
LGMN |
0.314 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272854 |
|
|
Homo sapiens |
MDA-MB-231 Cell |
pmid |
sentence |
24610907 |
We demonstrate that TRAF6 ubiquitinates the proform of AEP through K63-linked polyubiquitin, reversible by USP17, and forms a complex with HSP90α to subsequently promote pro-AEP intracellular stability as well as secretion. We now present evidence that AEP is a substrate for TRAF6 ubiquitination, resulting in AEP/TRAF6/HSP90α complex formation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRAF6 | up-regulates quantity by stabilization
polyubiquitination
|
LGMN |
0.312 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272853 |
|
|
Homo sapiens |
MDA-MB-231 Cell |
pmid |
sentence |
24610907 |
We demonstrate that TRAF6 ubiquitinates the proform of AEP through K63-linked polyubiquitin, reversible by USP17, and forms a complex with HSP90α to subsequently promote pro-AEP intracellular stability as well as secretion. We now present evidence that AEP is a substrate for TRAF6 ubiquitination, resulting in AEP/TRAF6/HSP90α complex formation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |