| + |
PRKN | down-regulates quantity by destabilization 
ubiquitination
|
HIF1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278542 |
Lys477 |
LNQEVALkLEPNPES |
Homo sapiens |
|
| pmid |
sentence |
| 29180628 |
These results indicate that Parkin inhibits HIF-1alpha transcriptional activity.|Ubiquitination of HIF-1alpha at lysine 477 by Parkin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | down-regulates
phosphorylation
|
HIF1A |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167476 |
Ser247 |
KTFLSRHsLDMKFSY |
Homo sapiens |
|
| pmid |
sentence |
| 20699359 |
In this work, we investigate the phosphorylation of the n-terminal heterodimerization (pas) domain of hif-1alpha and identify ser247 as a major site of in vitro modification by casein kinase 1delta (ck1delta). Mutation of this site to alanine, surprisingly, enhanced the transcriptional activity of hif-1alpha |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSK3B | down-regulates activity
phosphorylation
|
HIF1A |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278294 |
Ser551 |
TEAKNPFsTQDTDLD |
Homo sapiens |
|
| pmid |
sentence |
| 23210979 |
Glycogen synthase kinase 3 \u03b2 (GSK3\u03b2) phosphorylates HIF-1\u03b1 at three serine residues (Ser-551, Ser-555, and Ser-589) located within its oxygen-dependent degradation domain (ODDD) [12] (Figure 5). Phosphorylation at these residues by GSK3\u03b2 enhances HIF-1\u03b1 degradation in a pVHL-independent manner, resulting in suppression of the HIF-1 activity [12,13].|Phosphorylation at these residues by GSK3beta enhances HIF-1alpha degradation in a pVHL independent manner, resulting in suppression of the HIF-1 activity , ]. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK3 | down-regulates
phosphorylation
|
HIF1A |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178739 |
Ser576 |
DDDFQLRsFDQLSPL |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18519666 |
Polo-like kinase 3 functions as a tumor suppressor and is a negative regulator of hypoxia-inducible factor-1 alpha under hypoxic conditionsplk3 can potentially inhibit hif-1_ by physical interaction and direct phosphorylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178743 |
Ser657 |
ETTSATSsPYRDTQS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18519666 |
Polo-like kinase 3 functions as a tumor suppressor and is a negative regulator of hypoxia-inducible factor-1 alpha under hypoxic conditionsplk3 can potentially inhibit hif-1_ by physical interaction and direct phosphorylation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | up-regulates 
phosphorylation
|
HIF1A |
0.696 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178731 |
Ser641 |
DIKILIAsPSPTHIH |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18519666 |
We show that at least two different nuclear protein kinases, one of them identified as p42/p44 mapk, can modify hif-1_. Analysis of in vitro phosphorylated hif-1_ by mass spectroscopy revealed residues ser-641 and ser-643 as possible mapk phosphorylation sites these data suggest that phosphorylation of ser-641/643 by mapk promotes the nuclear accumulation and transcriptional activity of hif-1_ |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178735 |
Ser643 |
KILIASPsPTHIHKE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18519666 |
We show that at least two different nuclear protein kinases, one of them identified as p42/p44 mapk, can modify hif-1_. Analysis of in vitro phosphorylated hif-1_ by mass spectroscopy revealed residues ser-641 and ser-643 as possible mapk phosphorylation sites these data suggest that phosphorylation of ser-641/643 by mapk promotes the nuclear accumulation and transcriptional activity of hif-1_ |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | up-regulates
phosphorylation
|
HIF1A |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178723 |
Ser641 |
DIKILIAsPSPTHIH |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18519666 |
We show that at least two different nuclear protein kinases, one of them identified as p42/p44 mapk, can modify hif-1_. Analysis of in vitro phosphorylated hif-1_ by mass spectroscopy revealed residues ser-641 and ser-643 as possible mapk phosphorylation sites these data suggest that phosphorylation of ser-641/643 by mapk promotes the nuclear accumulation and transcriptional activity of hif-1_ |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178727 |
Ser643 |
KILIASPsPTHIHKE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18519666 |
We show that at least two different nuclear protein kinases, one of them identified as p42/p44 mapk, can modify hif-1_. Analysis of in vitro phosphorylated hif-1_ by mass spectroscopy revealed residues ser-641 and ser-643 as possible mapk phosphorylation sites these data suggest that phosphorylation of ser-641/643 by mapk promotes the nuclear accumulation and transcriptional activity of hif-1_ |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK1 | up-regulates activity
phosphorylation
|
HIF1A |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279599 |
Ser668 |
DTQSRTAsPNRAGKG |
Homo sapiens |
|
| pmid |
sentence |
| 24189531 |
In vitro kinase assays reveal that CDK1 directly phosphorylates HIF-1\u03b1 at a previously unidentified regulatory site, Ser668.|Overexpression of CDK1 and/or cyclin B1 is sufficient to stabilize HIF-1alpha under normoxic conditions, whereas inhibition of CDK1 enhances the proteasomal degradation of HIF-1alpha, reducing its half-life and steady-state levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5 | up-regulates activity
phosphorylation
|
HIF1A |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279020 |
Ser687 |
TEKSHPRsPNVLSVA |
Homo sapiens |
|
| pmid |
sentence |
| 27027353 |
In conclusion, we obtained compelling evidence that CDK5 directly stabilizes the transcription factor hypoxia inducible factor-1\u03b1 by phosphorylation, and thus promotes the formation of blood vessels.|Mass spectrometry and site directed mutagenesis revealed a stabilizing phosphorylation of HIF-1\u03b1 at Ser687 by CDK5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATM | up-regulates
phosphorylation
|
HIF1A |
0.434 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169999 |
Ser696 |
NVLSVALsQRTTVPE |
Homo sapiens |
|
| pmid |
sentence |
| 21095582 |
Here we show that hypoxia results in ataxia telangiectasia mutated (atm)-dependent phosphorylation of hypoxia-inducible factor 1-alpha (hif-1_) on serine(696) and mediates downregulation of mtorc1 signaling. phosphorylation of hif-1_ by atm is required for its stability |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIM1 | up-regulates quantity by stabilization
phosphorylation
|
HIF1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277311 |
Thr455 |
LAMSPLPtAETPKPL |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34211090 |
PIM1 kinase directly phosphorylates HIF-1α at threonine 455, a previously uncharacterized site within its oxygen-dependent degradation domain. This phosphorylation event disrupts the ability of prolyl hydroxylases to bind and hydroxylate HIF-1α, interrupting its canonical degradation pathway and promoting constitutive transcription of HIF-1 target genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 |
phosphorylation
|
HIF1A |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250891 |
Thr796 |
ESGLPQLtSYDCEVN |
in vitro |
|
| pmid |
sentence |
| 17382325 |
These results implied that only Thr-796 was phosphorylated CK2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HIF1A | down-regulates quantity by repression
transcriptional regulation
|
KDM1A |
0.266 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271573 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32938217 |
To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression 
transcriptional regulation
|
KDM4B |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263738 |
|
|
Homo sapiens |
T-47D Cell |
| pmid |
sentence |
| 20682797 |
Here, we show the histone demethylase JMJD2B is regulated by both ERalpha and HIF-1alpha, drives breast cancer cell proliferation in normoxia and hypoxia, and epigenetically regulates the expression of cell cycle genes such as CCND1, CCNA1, and WEE1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
PKG |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270291 |
|
|
Homo sapiens |
HeLa Cell, HEP-3B Cell |
| pmid |
sentence |
| 8089148 |
Hypoxia-inducible factor 1 (HIF-1) activates erythropoietin gene transcription in Hep3B cells subjected to hypoxia. HIF-1 activity is also induced by hypoxia in non-erythropoietin-producing cells, suggesting a more general regulatory role. We now report that RNAs encoding the glycolytic enzymes aldolase A (ALDA), phosphoglycerate kinase 1 (PGK1), and pyruvate kinase M were induced by exposure of Hep3B or HeLa cells to inducers of HIF-1 (1% O2, cobalt chloride, or desferrioxamine). Sequences from the ALDA, PFKL, and PGK1 genes containing HIF-1 binding sites mediated hypoxia-inducible transcription in transient expression assays. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
MMP2 |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281240 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23093058 |
After exposure to hypoxia, HIF-1α protein was up-regulated, both mRNA and protein levels of E-cadherin were down-regulated and MMP-2 was up-regulated, while HIF-1α mRNA showed no significant change. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281241 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23093058 |
After exposure to hypoxia, HIF-1α protein was up-regulated, both mRNA and protein levels of E-cadherin were down-regulated and MMP-2 was up-regulated, while HIF-1α mRNA showed no significant change. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
KDM3A |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271568 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32938217 |
To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | form complex 
binding
|
HIF-1 complex |
0.783 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267447 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27692180 |
HIF-1 consists of two subunits, HIF-1α and HIF-1β. While HIF-1β protein is constitutively expressed and present in excess, HIF-1α protein has a short half-life |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
PGK1 |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254424 |
|
|
Homo sapiens |
HeLa Cell, HEP-3B Cell |
| pmid |
sentence |
| 8089148 |
Hypoxia-inducible factor 1 (HIF-1) activates erythropoietin gene transcription in Hep3B cells subjected to hypoxia. HIF-1 activity is also induced by hypoxia in non-erythropoietin-producing cells, suggesting a more general regulatory role. We now report that RNAs encoding the glycolytic enzymes aldolase A (ALDA), phosphoglycerate kinase 1 (PGK1), and pyruvate kinase M were induced by exposure of Hep3B or HeLa cells to inducers of HIF-1 (1% O2, cobalt chloride, or desferrioxamine). Sequences from the ALDA, PFKL, and PGK1 genes containing HIF-1 binding sites mediated hypoxia-inducible transcription in transient expression assays. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
KDM2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271566 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32938217 |
To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity
transcriptional regulation
|
EPO |
0.645 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256593 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8756616 |
We demonstrate the involvement of HIF-1 in the activation of VEGF transcription. VEGF 5'-flanking sequences mediated transcriptional activation of reporter gene expression in hypoxic Hep3B cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
ABCB1 |
0.303 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254420 |
|
|
Homo sapiens |
Microvascular Endothelial Cell |
| pmid |
sentence |
| 12067980 |
Examination of the MDR1 gene identified a binding site for hypoxia inducible factor-1 (HIF-1), and inhibition of HIF-1 expression by antisense oligonucleotides resulted in significant inhibition of hypoxia-inducible MDR1 expression and a nearly complete loss of basal MDR1 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EML4-ALK | up-regulates quantity by stabilization
|
HIF1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259173 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27141364 |
EML4-ALK enhanced HIF-1α expression through increasing transcription and decreasing ubiquitination of HIF-1α. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates
|
Epithelial-mesenchymal_transition |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254768 |
|
|
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 27476001 |
Our present study reveals that DAB2IP prevents EMT and metastasis of prostate cancer through targeting PROX1 gene transcription and destabilizing HIF1α protein, which provides a new insight into mechanism that DAB2IP regulates EMT and PCa metastasis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SIAH2 | up-regulates
|
HIF1A |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149893 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17003045 |
The ring finger ubiquitin ligase siah2 controls the stability of various substrates involved in stress and hypoxia responses, including the phd3, which controls the stability of hif-1alpha |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGLN3 | down-regulates quantity by destabilization
hydroxylation
|
HIF1A |
0.797 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262000 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24990963 |
There are three EglN family members in humans and mice (EglN1, EglN2, and EglN3). Their enzymatic activity requires oxygen, ascorbic acid, iron, and α-ketoglutarate (α-KG). Under hypoxic conditions, EglNs lose their activity and fail to hydroxylate HIFα, which leads to HIFα stabilization |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
STC2 |
0.298 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260389 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18394600 |
With the ChIP assay, we demonstrated the direct binding of HIF-1alpha to STC2 promoter. These findings support the notion that HIF-1 is a potent stimulator of STC2 expression. Collectively, this is the first report to show that STC2 was aberrantly hypermethylated in human cancer cells. The findings demonstrated that STC2 epigenetic inactivation may interfere with HIF-1 mediated activation of STC2 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RWDD3 | up-regulates
sumoylation
|
HIF1A |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158590 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17956732 |
Rsume,_a small_rwd-containing protein, enhances sumo conjugation and stabilizes hif-1alpha during hypoxia |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PROX1 | up-regulates quantity by stabilization
|
HIF1A |
0.258 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254766 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27476001 |
PROX1 is important to maintain HIF1α protein stability by inhibiting the proteasome activity after DAB2IP loss, since our immunoprecipitation data showed that knocking-down PROX1 could enhance the protein–protein interaction between HIF1α and ubiquitin in DAB2IP-deficient LAPC-4 and RWPE-1 KD cells. we found that knocking-down PROX1 could decrease HIF1α protein stability, because HIF1α protein degradation was significantly blocked by MG132 treatment in LAPC-4 and RWPE-1 KD cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EML4-ALK | up-regulates quantity by expression
transcriptional regulation
|
HIF1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259172 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27141364 |
EML4-ALK enhanced HIF-1α expression through increasing transcription and decreasing ubiquitination of HIF-1α. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
KDM6B |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271571 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32938217 |
To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KDM4C | up-regulates activity
binding
|
HIF1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263873 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29207681 |
In hypoxia, HIF-1α dimerizes with HIF-1β to form active HIF-1 complex. JMJD2C interacts with HIF-1α and promotes the transcriptional activation of HIF-1 targeting genes via demethylating di- and trimethylated H3K9. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
ubiquitination
|
HIF1A |
0.376 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271426 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19940151 |
the ubiquitin ligase activity of CHIP regulates HIF-1α degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGLN1 | down-regulates quantity by destabilization
hydroxylation
|
HIF1A |
0.917 |
| 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 |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
KDM5B |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271563 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32938217 |
To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
CD274 |
0.283 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259092 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27141364 |
STAT3 and HIF-1α cooperatively enhance PD-L1 expression in EML4-ALK-translocated pADC cells under hypoxia. Taken together, these findings suggest that EML4-ALK might increase HIF-1α expression under hypoxia by enhancing transcription and inhibiting ubiquitination of HIF-1α, resulting in the stabilization of HIF-1α, consequently contributing to HIF-1α-mediated upregulation of PD-L1 under hypoxia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
2-oxoglutarate(2-) | up-regulates activity
chemical activation
|
HIF1A |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253138 |
|
|
|
|
| pmid |
sentence |
| 20383689 |
HIF prolyl hydroxylase-3 mediates alpha-ketoglutarate-induced apoptosis and tumor suppression|The hypoxia inducible factor (HIF) prolyl hydroxylases (PHDs) are enzymes that are functionally inactivated in hypoxia, as they use both oxygen and alpha-ketoglutarate as substrates to hydroxylate target prolyl residues. |
|
| Publications: |
1 |
| + |
mTORC1 | up-regulates
|
HIF1A |
0.363 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167187 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20670887 |
Hif1alfa is the transcription factor downstream of mtorc1 in the control of glycolytic genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
KDM2B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271567 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32938217 |
To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF7 | down-regulates activity
ubiquitination
|
HIF1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271450 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23136067 |
SAG (Sensitive to Apoptosis Gene), also known as RBX2 (RING box protein 2), ROC2 (Regulator of Cullins 2), or RNF7 (RING Finger Protein 7), was originally cloned in our laboratory as a redox inducible antioxidant protein and later characterized as the second member of the RBX/ROC RING component of the SCF (SKP1-CUL-F-box Proteins) E3 ubiquitin ligase. by forming a complex with other components of the SCF E3 ligase, SAG promotes ubiquitination and degradation of a number of protein substrates, including c-JUN, DEPTOR, HIF-1α, IκBα, NF1, NOXA, p27, and procaspase-3, thus regulating various signaling pathways and biological processes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity
transcriptional regulation
|
VEGFA |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256592 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8387214 |
Transcription of the human erythropoietin (EPO) gene is activated in Hep3B cells exposed to hypoxia. Hypoxia-inducible factor 1 (HIF-1) is a nuclear factor whose DNA binding activity is induced by hypoxia in Hep3B cells, and HIF-1 binds at a site in the EPO gene enhancer that is required for hypoxic activation of transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | NOTCH Signaling |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
KDM4B |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271569 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32938217 |
To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
IL1B |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251718 |
|
|
Mus musculus |
Macrophage |
| pmid |
sentence |
| 24352507 |
We finally confirmed that in the absence of HIF-1α there was a significant reduction at the protein level in pro-caspase-1, activated caspase-1, pro-IL-1β, and ultimately active IL-1β (Fig. 4g and h). These data show that adenosine induced up-regulation of IL-1β is dependent on a CREB/HIF-1α pathway which is distinct from the NF-kB pathway used for initial production of IL-1β in response to LPS. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256236 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 25750431 |
The results of this study show that the absence of HIFs in MPs has no impact on the resolution of inflammation in two sterile models of skeletal muscle regeneration |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256235 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 17548584 |
The loss of macrophage expression of HIF-1 led to significant decreases in the production of TNF-a, IL-1a, IL-1b, and IL-12 |
|
| Publications: |
3 |
Organism: |
Mus Musculus |
| + |
RBPJ/NOTCH | up-regulates quantity by expression
transcriptional regulation
|
HIF1A |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209720 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19808903 |
We report a Notch signal-induced pathway that leads to transcriptional activation of HIF1-alpha gene. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | NOTCH Signaling |
| + |
NatA | down-regulates quantity by destabilization
acetylation
|
HIF1A |
0.515 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267226 |
|
|
Homo sapiens |
HT-1080 Cell |
| pmid |
sentence |
| 12464182 |
In this report, we reveal an important function for ARD1 in mammalian cells as a protein acetyltransferase by direct binding to HIF-1alpha to regulate its stability. We present further evidence showing that ARD1-mediated acetylation enhances interaction of HIF-1alpha with pVHL and HIF-1alpha ubiquitination, suggesting that the acetylation of HIF-1alpha by ARD1 is critical to proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
ALDOA |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254422 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8955077 |
we characterize hypoxia response elements in the promoters of the ALDA, ENO1, and Ldha genes. Our data establish that functional hypoxia-response elements consist of a pair of contiguous transcription factor binding sites at least one of which contains the core sequence 5'-RCGTG-3' and is recognized by HIF-1. These results provide further evidence that the coordinate transcriptional activation of genes encoding glycolytic enzymes which occurs in hypoxic cells is mediated by HIF-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOTCH1 | up-regulates activity
relocalization
|
HIF1A |
0.648 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141315 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16256737 |
The notch intracellular domain interacts with hif-1alpha and hif-1alpha is recruited to notch-responsive promoters upon notch activation under hypoxic conditions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | NOTCH Signaling |
| + |
HIF1A | up-regulates
|
Glycolysis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259380 |
|
|
Homo sapiens |
Synovial Fibroblast |
| pmid |
sentence |
| 28623342 |
Our results demonstrate that SF(synovial fibroblasts) are highly dependent on glycolytic metabolism and that HIF-1α plays a regulatory role in glycolysis even under aerobic conditions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259381 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17415528 |
HIF-1 has been known as a major transcription factor for the induction of virtually all genes encoding glucose transporters and glycolytic enzymes, which allows hypoxic tumor cells to take up glucose more efficiently and metabolize pyruvate to lactate |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ATP6AP1 | down-regulates quantity by destabilization 
|
HIF1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261347 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28296633 |
Depletion or inhibition of the V-ATPase stabilises HIF1α in aerobic conditions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | down-regulates quantity by repression
transcriptional regulation
|
TM9SF4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266705 |
|
|
Homo sapiens |
Acute Myeloid Leukemia Cell |
| pmid |
sentence |
| 25961573 |
Here, we investigated the impact of hypoxia on TM9SF4 expression in leukemic cells and identified TM9SF4 as a direct target of HIF-1α, downregulated in these cells by hypoxia. Then, we found that the hypoxia-mediated downregulation of TM9SF4 expression is associated with a decrease of cell adhesion of leukemic cells to fibronectin, thus demonstrating that human TM9SF4 is a new molecule involved in leukemic cell adhesion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CEP41 | up-regulates activity
binding
|
HIF1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269662 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 31885126 |
We performed these assays in HEK 293T cells and observed CEP41 binds HIF1α under both normoxic and hypoxic conditions. Of note, we found hypoxia induces more expression of HIF1α and increases its binding to CEP41 (Fig 8B and C). Hence, these results suggest CEP41 modulates the activation of HIF1α via a physical interaction |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
P4HA1 | up-regulates activity
|
HIF1A |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279875 |
|
|
|
|
| pmid |
sentence |
| 31239153 |
P4HA1 regulates HIF1a activity in pancreatic cancer. P4HA1 can also increase HIF1a protein level in PDAC cells indicative of a positive feedback loop between P4HA1 and HIF1a. |
|
| Publications: |
1 |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
KDM5A |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271565 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32938217 |
To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | NOTCH Signaling |
| + |
XIAP | up-regulates activity
ubiquitination
|
HIF1A |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278740 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28666324 |
HIF1alpha is ubiquitinated by XIAP.|Lys 63 -linked ubiquitination of HIF1alpha by XIAP is dependent on the activity of E2 ubiquitin conjugating enzyme Ubc13.|We find that XIAP and Ubc13 dependent Lys 63 -linked polyubiquitination promotes HIF1alpha nuclear retention leading to an increase in the expression of HIF1 responsive genes.|The data indicate that XIAP promotes the formation of the non-degradative Lys63-linked ubiquitin chains onto hypoxia inducible factor1\u03b1, but does not affect the formation of Lys48-linked chains. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | up-regulates
phosphorylation
|
HIF1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270191 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18519666 |
We show that at least two different nuclear protein kinases, one of them identified as p42/p44 mapk, can modify hif-1_. Analysis of in vitro phosphorylated hif-1_ by mass spectroscopy revealed residues ser-641 and ser-643 as possible mapk phosphorylation sites these data suggest that phosphorylation of ser-641/643 by mapk promotes the nuclear accumulation and transcriptional activity of hif-1_ |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF3A | down-regulates quantity by repression
transcriptional regulation
|
HIF1A |
0.52 |
| 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 |
| + |
DAB2IP | down-regulates quantity by destabilization
|
HIF1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254765 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27476001 |
DAB2IP destabilizes HIF1α protein to inhibit EMT in PCa cells. DAB2IP may destabilize HIF1α protein in PCa cells via an ubiquitin-proteasome system. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
PDK1 |
0.473 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267444 |
|
|
Homo sapiens |
P493-6 Cell |
| pmid |
sentence |
| 16517405 |
Activation of glycolytic genes by HIF-1 is considered critical for metabolic adaptation to hypoxia through increased conversion of glucose to pyruvate and subsequently to lactate. We found that HIF-1 also actively suppresses metabolism through the tricarboxylic acid cycle (TCA) by directly trans-activating the gene encoding pyruvate dehydrogenase kinase 1 (PDK1). PDK1 inactivates the TCA cycle enzyme, pyruvate dehydrogenase (PDH), which converts pyruvate to acetyl-CoA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
NT5E |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254423 |
|
|
Homo sapiens |
Epithelial Cell |
| pmid |
sentence |
| 12370277 |
Examination of the CD73 gene promoter identified at least one binding site for hypoxia-inducible factor-1 (HIF-1) and inhibition of HIF-1alpha expression by antisense oligonucleotides resulted in significant inhibition of hypoxia-inducible CD73 expression |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
FAM162A |
0.283 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260292 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15082785 |
In this work, we report the identification of an HIF-1 alpha-responsive proapoptotic molecule, HGTD-P. Its expression was directly regulated by HIF-1 alpha through a hypoxia-responsive element on the HGTD-P promoter region. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGLN2 | down-regulates quantity by destabilization
hydroxylation
|
HIF1A |
0.855 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261999 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24990963 |
There are three EglN family members in humans and mice (EglN1, EglN2, and EglN3). Their enzymatic activity requires oxygen, ascorbic acid, iron, and α-ketoglutarate (α-KG). Under hypoxic conditions, EglNs lose their activity and fail to hydroxylate HIFα, which leads to HIFα stabilization |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
EPO |
0.645 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253695 |
|
|
|
|
| pmid |
sentence |
| 8663540 |
Hypoxia-inducible factor 1 (HIF-1) is a heterodimeric basic helix-loop-helix transcription factor that regulates hypoxia-inducible genes including the human erythropoietin (EPO) gene. |
|
| Publications: |
1 |
| + |
HIF1A | up-regulates
|
Metabolism |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256591 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17415528 |
HIF-1 has been known as a major transcription factor for the induction of virtually all genes encoding glucose transporters and glycolytic enzymes, which allows hypoxic tumor cells to take up glucose more efficiently and metabolize pyruvate to lactate |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
KDM5C |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271564 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32938217 |
To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
Aldolase |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270229 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8955077 |
we characterize hypoxia response elements in the promoters of the ALDA, ENO1, and Ldha genes. Our data establish that functional hypoxia-response elements consist of a pair of contiguous transcription factor binding sites at least one of which contains the core sequence 5'-RCGTG-3' and is recognized by HIF-1. These results provide further evidence that the coordinate transcriptional activation of genes encoding glycolytic enzymes which occurs in hypoxic cells is mediated by HIF-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SENP1 | up-regulates
desumoylation
|
HIF1A |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158891 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17981124 |
Sumo-specific protease 1 is essential for stabilization of hif1alpha during hypoxia / our results support a model in which sumoylated hif1_ is unstable but can be stabilized when sumo is removed by senp1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | up-regulates
phosphorylation
|
HIF1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270095 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18519666 |
We show that at least two different nuclear protein kinases, one of them identified as p42/p44 mapk, can modify hif-1_. Analysis of in vitro phosphorylated hif-1_ by mass spectroscopy revealed residues ser-641 and ser-643 as possible mapk phosphorylation sites these data suggest that phosphorylation of ser-641/643 by mapk promotes the nuclear accumulation and transcriptional activity of hif-1_ |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
ALAS2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254421 |
|
|
Homo sapiens |
K-562 Cell |
| pmid |
sentence |
| 21207956 |
Hypoxia-induced expression of erythroid-specific ALAS2 is mediated by HIF1 in erythroid cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Hypoxia | up-regulates activity
|
HIF1A |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279878 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11248550 |
The HIF-1α subunit is subjected to oxygen-dependent ubiquitination and proteasomal degradation that is mediated by the von Hippel-Lindau protein. Interaction of HIF-1α transactivation domains with coactivators is induced by hypoxia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
KDM7A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271572 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32938217 |
To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARNT | up-regulates activity
binding
|
HIF1A |
0.783 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253720 |
|
|
|
|
| pmid |
sentence |
| 14764593 |
The functional transcription factor exists as a heterodimeric complex consisting of HIF-1alpha and the aryl hydrocarbon receptor nuclear translocator (ARNT). Association of HIF-1 with ARNT is required for its activity; however, no other role has been ascribed to this interaction. |
|
| Publications: |
1 |
| + |
MAPK14 | up-regulates
|
HIF1A |
0.309 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149887 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17003045 |
The ring finger ubiquitin ligase siah2 controls the stability of various substrates involved in stress and hypoxia responses, including the phd3, which controls the stability of hif-1alpha. In the present study we determined the role of siah2 phosphorylation in the regulation of its activity toward phd3. We show that siah2 is subject to phosphorylation by p38 mapk, which increases siah2-mediated degradation of phd3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MDM2 | down-regulates quantity by destabilization
ubiquitination
|
HIF1A |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271385 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 10640274 |
We find that p53 promotes Mdm2-mediated ubiquitination and proteasomal degradation of the HIF-1alpha subunit of hypoxia-inducible factor 1 (HIF-1), a heterodimeric transcription factor that regulates cellular energy metabolism and angiogenesis in response to oxygen deprivation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
KDM4C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271570 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32938217 |
To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBP1 | down-regulates activity
binding
|
HIF1A |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267590 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30616754 |
FBP1, but not FBP2, suppresses HIF-1a activity by directly binding to its inhibitory domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
CCL2 |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251719 |
|
|
Homo sapiens |
Perivascular Astrocyte |
| pmid |
sentence |
| 17474992 |
These findings suggest that both MCP-1 and MCP-5 are HIF-1 target genes and that HIF-1α is involved in transcriptional induction of these two chemokines in astrocytes by hypoxia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
P4HA1 |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279840 |
|
|
Homo sapiens |
Pancreatic Ductal Adenocarcinoma Cell |
| pmid |
sentence |
| 40332386 |
Hypoxia upregulates P4HA1 expression in PDAC PDOs through HIF1α. Our results show that the treatment of PDO4 and PDO11 cells with 10 μmol/L of PX-478 for 24 hours reduced the levels of P4HA1 in hypoxia (Fig. 2F), suggesting P4HA1 expression in hypoxia is regulated by HIF1α expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
TWIST1 |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281239 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18635960 |
Hypoxia Promotes Cancer Metastasis throughthe Induction of EMT. Regulation of TWIST Expression by HIF-1 and its Critical Rolein Hypoxia Mediated EMT. Repressionof endogenous HIF-1αby siRNA in cells under hypoxia revertedtheTWISTlevels to pre-hypoxic status, demonstrating that HIF-1αis the major regulator ofTWISTexpression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
HIF1A
- 
- 