| + |
heme | up-regulates activity 
chemical activation
|
FBXO22 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259332 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31257023 |
Here, we show that heme triggers the degradation of Bach1, a pro-metastatic transcription factor, by promoting its interaction with the ubiquitin ligase Fbxo22. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HMOX2 | down-regulates quantity 
chemical modification
|
heme |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251912 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10490932 |
Heme oxygenase (HO), by catabolizing heme to bile pigments, down-regulates cellular hemoprotein, hemoglobin, and heme |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
heme | up-regulates activity
chemical activation
|
HBA1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251909 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26557657 |
Heme is a prosthetic group comprising ferrous iron (Fe2+) and protoporphyrin IX and is an essential cofactor in various biological processes such as oxygen transport (hemoglobin) and storage (myoglobin) and electron transfer (respiratory cytochromes) in addition to its role as a structural component of hemoproteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
heme | up-regulates activity
chemical activation
|
HBB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251908 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26557657 |
Heme is a prosthetic group comprising ferrous iron (Fe2+) and protoporphyrin IX and is an essential cofactor in various biological processes such as oxygen transport (hemoglobin) and storage (myoglobin) and electron transfer (respiratory cytochromes) in addition to its role as a structural component of hemoproteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HMOX1 | down-regulates quantity
chemical modification
|
heme |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251911 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10490932 |
Heme oxygenase (HO), by catabolizing heme to bile pigments, down-regulates cellular hemoprotein, hemoglobin, and heme |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259333 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16115609 |
The microsomal heme oxygenase system consists of heme oxygenase (HO) and NADPH-cytochrome P450 reductase, and plays a key role in the physiological catabolism of heme which yields biliverdin, carbon monoxide, and iron as the final products. Heme degradation proceeds essentially as a series of autocatalytic oxidation reactions involving heme bound to HO |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
STC2/HMOX1 | down-regulates quantity by destabilization
|
heme |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260405 |
|
|
|
|
| pmid |
sentence |
| 22503972 |
Stanniocalcin 2, forms a complex with heme oxygenase 1, binds hemin and is a heat shock protein.|Taken together, our findings point to three novel functions of STC2, and suggest that STC2 interacts with HO1 to form a eukaryotic 'stressosome' involved in the degradation of heme. |
|
| Publications: |
1 |
| + |
SLC46A1 | up-regulates quantity
relocalization
|
heme |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268265 |
|
|
Homo sapiens |
Hepatocyte |
| pmid |
sentence |
| 32621820 |
SLC46A1 contributes to hepatic iron metabolism by importing heme in hepatocytes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
heme