+ |
PINK1 | down-regulates activity
phosphorylation
|
HIF3A |
0.355 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263090 |
Thr12 |
LQRARSTtELRKEKS |
Homo sapiens |
SH-SY5Y Cell |
pmid |
sentence |
27551449 |
Here we show that IPAS is a key molecule involved in neuronal cell death in Parkinson's disease (PD). IPAS was ubiquitinated by Parkin for proteasomal degradation following carbonyl cyanide m-chlorophenyl hydrazone treatment. Phosphorylation of IPAS at Thr12 by PTEN-induced putative kinase 1 (PINK1) was required for ubiquitination to occur. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HIF3A | down-regulates quantity by repression
transcriptional regulation
|
EPAS1 |
0.508 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261616 |
|
|
Homo sapiens |
HEP-3B Cell |
pmid |
sentence |
21479871 |
None of the long HIF-3α variants was capable of efficient induction of an HRE reporter in overexpression experiments, but instead inhibited the transcriptional activation of the reporter by HIF-1 and HIF-2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKN | down-regulates quantity by destabilization
ubiquitination
|
HIF3A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263089 |
|
|
Homo sapiens |
SH-SY5Y Cell |
pmid |
sentence |
27551449 |
Here we show that IPAS is a key molecule involved in neuronal cell death in Parkinson's disease (PD). IPAS was ubiquitinated by Parkin for proteasomal degradation following carbonyl cyanide m-chlorophenyl hydrazone treatment. Phosphorylation of IPAS at Thr12 by PTEN-induced putative kinase 1 (PINK1) was required for ubiquitination to occur. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HIF3A | down-regulates quantity by repression
transcriptional regulation
|
HIF1A |
0.503 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261615 |
|
|
Homo sapiens |
HEP-3B Cell |
pmid |
sentence |
21479871 |
None of the long HIF-3α variants was capable of efficient induction of an HRE reporter in overexpression experiments, but instead inhibited the transcriptional activation of the reporter by HIF-1 and HIF-2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |