+ |
Hypoxia | down-regulates
|
EGLN1 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261995 |
|
|
Homo sapiens |
|
pmid |
sentence |
32755251 |
Under hypoxic conditions, PHD2 activity is limited, and therefore HIF-1α protein is stabilized, leading to an increase in the transcription of erythropoietin as well as hundreds of target genes that coordinate diverse processes |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EIF2S2 | up-regulates quantity
translation regulation
|
EGLN1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266386 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
29530922 |
DAP5 is involved in PHD2 translation. Distinct responses to DAP5 depletion (under hypoxia) of primary MEFs versus malignant glioma cells suggest that DAP5-mediated control of PHD2 may have special significance in cancer. Neoplastic cells may exploit DAP5 for managing chronic oxygen deprivation, possibly contributing to their adaptation to growth/proliferation under hypoxia. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
dimethyloxalylglycine | down-regulates activity
chemical inhibition
|
EGLN1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261991 |
|
|
Homo sapiens |
A-549 Cell |
pmid |
sentence |
28900510 |
We treated the A549 cells with the following EGLN/PHD inhibitors: dimethyloxalyglycine (DMOG), CoCl2, inhibitors of dioxygenases, and BAY 85-3494 (BAY), a specific inhibitor of EGLNs with highest potency against EGLN1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EGLN1 | down-regulates quantity by destabilization
hydroxylation
|
HIF1A |
0.918 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261994 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
32755251 |
Hypoxia-inducible factor-1 (HIF-1) is a key regulator of erythropoiesis. In this article, we report 3 novel mutations, P378S, A385T, and G206C, on the EGLN1 gene encoding the negative HIF-1α regulator prolyl hydroxylase domain-2 (PHD2) in 3 patients with isolated erythrocytosis. These mutations impair PHD2 protein stability and partially reduce PHD2 activity, leading to increased HIF-1α protein levels in cultured cells.|Oxygen-dependent hydroxylation by the prolyl hydroxylase domain-2 (PHD2) protein marks HIF-1alpha for ubiquitination by the von Hippel Lindau (VHL) tumor suppressor protein, leading to proteasomal degradation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |