| + |
MAPK1 | up-regulates activity 
phosphorylation
|
PPARA |
0.579 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249433 |
Ser12 |
ESPLCPLsPLEAGDL |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 10187842 |
We now demonstrate that amino acids 1-92 of hPPARalpha contain an activation function (AF)-1-like domain, which is further activated by insulin through a pathway involving the mitogen-activated protein kinases p42 and p44. Further analysis of the amino-terminal region of PPARalpha revealed that the insulin-induced trans-activation occurs through the phosphorylation of two mitogen-activated protein kinase sites at positions 12 and 21, both of which are conserved across evolution. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249434 |
Ser21 |
LEAGDLEsPLSEEFL |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 10187842 |
We now demonstrate that amino acids 1-92 of hPPARalpha contain an activation function (AF)-1-like domain, which is further activated by insulin through a pathway involving the mitogen-activated protein kinases p42 and p44. Further analysis of the amino-terminal region of PPARalpha revealed that the insulin-induced trans-activation occurs through the phosphorylation of two mitogen-activated protein kinase sites at positions 12 and 21, both of which are conserved across evolution. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | up-regulates activity
phosphorylation
|
PPARA |
0.602 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249473 |
Ser12 |
ESPLCPLsPLEAGDL |
Homo sapiens |
|
| pmid |
sentence |
| 10187842 |
We now demonstrate that amino acids 1-92 of hPPARalpha contain an activation function (AF)-1-like domain, which is further activated by insulin through a pathway involving the mitogen-activated protein kinases p42 and p44. Further analysis of the amino-terminal region of PPARalpha revealed that the insulin-induced trans-activation occurs through the phosphorylation of two mitogen-activated protein kinase sites at positions 12 and 21, both of which are conserved across evolution. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249474 |
Ser21 |
LEAGDLEsPLSEEFL |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 10187842 |
We now demonstrate that amino acids 1-92 of hPPARalpha contain an activation function (AF)-1-like domain, which is further activated by insulin through a pathway involving the mitogen-activated protein kinases p42 and p44. Further analysis of the amino-terminal region of PPARalpha revealed that the insulin-induced trans-activation occurs through the phosphorylation of two mitogen-activated protein kinase sites at positions 12 and 21, both of which are conserved across evolution. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
GSK3A | up-regulates activity
phosphorylation
|
PPARA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277431 |
Ser280 |
FHCCQCTsVETVTEL |
Rattus norvegicus |
Cardiomyocyte Cell Line |
| pmid |
sentence |
| 30745182 |
Fatty acids (FAs) upregulate GSK-3α, which phosphorylates PPARα at Ser280 in the ligand-binding domain (LBD). This modification ligand independently enhances transcription of a subset of PPARα targets, selectively stimulating FA uptake and storage, but not oxidation, thereby promoting lipid accumulation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278515 |
Ser280 |
FHCCQCTsVETVTEL |
Homo sapiens |
|
| pmid |
sentence |
| 30745182 |
GSK-3alpha phosphorylates PPARalpha at Ser280, located in the ligand binding domain.|These results suggest that GSK-3alpha positively regulates PPARalpha activity through Ser280 phosphorylation. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus, Homo Sapiens |
| + |
PPARA | up-regulates quantity by expression
transcriptional regulation
|
ARNTL |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268024 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 16556735 |
We demonstrate that PPARalpha plays a specific role in the peripheral circadian control because it is required to maintain the circadian rhythm of the master clock gene brain and muscle Arnt-like protein 1 (bmal1) in vivo. This regulation occurs via a direct binding of PPARalpha on a potential PPARalpha response element located in the bmal1 promoter. Reversely, BMAL1 is an upstream regulator of PPARalpha gene expression. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Circadian clock |
| + |
ERK1/2 | up-regulates activity
phosphorylation
|
PPARA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270180 |
|
|
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 10187842 |
We now demonstrate that amino acids 1-92 of hPPARalpha contain an activation function (AF)-1-like domain, which is further activated by insulin through a pathway involving the mitogen-activated protein kinases p42 and p44. Further analysis of the amino-terminal region of PPARalpha revealed that the insulin-induced trans-activation occurs through the phosphorylation of two mitogen-activated protein kinase sites at positions 12 and 21, both of which are conserved across evolution. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Monobutylphthalate | up-regulates activity
chemical activation
|
PPARA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268750 |
|
|
Homo sapiens |
Breast Cell Line |
| pmid |
sentence |
| 16326050 |
Mono(2-ethylhexyl)phthalate and mono-n-butyl phthalate activation of peroxisome proliferator activated-receptors alpha and gamma in breast |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPARA | up-regulates quantity by expression 
transcriptional regulation
|
CPT1A |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255047 |
|
|
Homo sapiens |
Caki-1 Cell |
| pmid |
sentence |
| 17150915 |
To investigate the intimate function of PPARalpha in the kidney, we analyzed the target gene expression in human metastatic renal cell carcinoma cell line, Caki-1, using small interfering RNA (siRNA) against PPARalpha and real-time RT-PCR methods. We found that some selected genes (long-chain fatty-acid-CoA ligase (FACL1), carnitine palmitoyltransferase 1A (CPT1A), adipose differentiation-related protein (ADRP) and aquaporin 3 (AQP3)) were down-regulated by PPARalpha siRNA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
gemfibrozil | up-regulates activity
chemical activation
|
PPARA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258318 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21889235 |
The combination of stilbene scaffold and gemfibrozil enhances the PPARα agonistic activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
perfluorooctanoic acid | up-regulates activity
chemical activation
|
PPARA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268753 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 35370244 |
Detailed in vitro studies on the effects of perfluorooctanoic acid (PFOA) have demonstrated that activation of peroxisome proliferator-activated receptor α (PPARα) is a key process by which PFOA affects the malignancy of estrogen receptor α (ERα)-positive breast cancer cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268790 |
|
|
Mus musculus |
3T3-L1 Cell |
| pmid |
sentence |
| 16731579 |
Human, mouse, and rat PPARα were activated by PFOA isomers and PFOS. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| + |
perfluorooctane-1-sulfonic acid | up-regulates activity
chemical activation
|
PPARA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268789 |
|
|
Mus musculus |
3T3-L1 Cell |
| pmid |
sentence |
| 16731579 |
Human, mouse, and rat PPARα were activated by PFOA isomers and PFOS. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268754 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 34861291 |
Perfluorooctane sulfonate (PFOS) is a stable environmental contaminant that can activate peroxisome proliferator-activated receptor alpha (PPARα). These results indicate that mouse PPARα can be activated in the liver by PFOS causing increased expression of Acox1, Cyp4a10 and histopathological changes in the liver. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| Tissue: |
Liver |
| + |
monoisononyl phthalate | up-regulates activity
chemical activation
|
PPARA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268780 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 27551952 |
MEHP and MiNP exhibit potent activation of hCAR2 and hPXR with higher affinities for these receptors than for the hPPARs. The rank order potency for MEHP and MiNP was hCAR2 > hPXR > hPPARs. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PPARA | up-regulates quantity by expression
transcriptional regulation
|
PLIN2 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255046 |
|
|
Homo sapiens |
Caki-1 Cell |
| pmid |
sentence |
| 17150915 |
To investigate the intimate function of PPARalpha in the kidney, we analyzed the target gene expression in human metastatic renal cell carcinoma cell line, Caki-1, using small interfering RNA (siRNA) against PPARalpha and real-time RT-PCR methods. We found that some selected genes (long-chain fatty-acid-CoA ligase (FACL1), carnitine palmitoyltransferase 1A (CPT1A), adipose differentiation-related protein (ADRP) and aquaporin 3 (AQP3)) were down-regulated by PPARalpha siRNA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STAT6 | up-regulates quantity by expression
transcriptional regulation
|
PPARA |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249534 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 20508200 |
Phosphorylated STAT6 dimerizes and translocates to the nucleus where it induces the expression of its target genes, including markers (Arg1, Chi3l3, Mrc1, Mgl1, and Retnla) and regulators (Pparalpha, Ppargamma and PGC-1?) of alternative activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mono(2-ethylhexyl) phthalate | up-regulates activity
chemical activation
|
PPARA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268745 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19433246 |
Phthalates are true ligands of PPARs. Mono-ethyl-hexyl-phthalate (MEHP), a metabolite of the widespread plasticizer di-ethyl-hexyl-phthalate (DEHP), has been found in exposed organisms and interacts with all three PPARs. A thorough analysis of its interactions with PPARgamma identified MEHP as a selective PPARgamma modulator, and thus a possible contributor to the obesity epidemic. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268749 |
|
|
in vitro |
|
| pmid |
sentence |
| 16326050 |
Mono(2-ethylhexyl)phthalate and mono-n-butyl phthalate activation of peroxisome proliferator activated-receptors alpha and gamma in breast |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268783 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 27551952 |
MEHP and MiNP exhibit potent activation of hCAR2 and hPXR with higher affinities for these receptors than for the hPPARs. The rank order potency for MEHP and MiNP was hCAR2 > hPXR > hPPARs. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, In Vitro, Chlorocebus Aethiops |
| + |
PPARA | up-regulates quantity by expression
transcriptional regulation
|
ACSL1 |
0.555 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255044 |
|
|
Homo sapiens |
Caki-1 Cell |
| pmid |
sentence |
| 17150915 |
To investigate the intimate function of PPARalpha in the kidney, we analyzed the target gene expression in human metastatic renal cell carcinoma cell line, Caki-1, using small interfering RNA (siRNA) against PPARalpha and real-time RT-PCR methods. We found that some selected genes (long-chain fatty-acid-CoA ligase (FACL1), carnitine palmitoyltransferase 1A (CPT1A), adipose differentiation-related protein (ADRP) and aquaporin 3 (AQP3)) were down-regulated by PPARalpha siRNA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RXRA | up-regulates
binding
|
PPARA |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105345 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11237216 |
Although the three ppar subtypes are closely related and bind to similar dna response elements as heterodimers with the 9-cis retinoic acid receptor rxr, each subserves a distinct physiology |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPARA | up-regulates
|
Fatty_acid_oxidation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268027 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18836859 |
PPAR-α is predominantly expressed in the liver and skeletal muscles, participating in fatty-acids catabolism. PPAR-α also activates fatty-acid oxidation in the kidney, skeletal muscles, and heart |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle, Kidney |
| Pathways: | Circadian clock |
| + |
KDM3B | up-regulates quantity by expression
transcriptional regulation
|
PPARA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266637 |
|
|
Mus musculus |
HIB-1B Cell |
| pmid |
sentence |
| 19194461 |
We show that Jhdm2a expression is induced by beta-adrenergic stimulation, and that Jhdm2a directly regulates peroxisome proliferator-activated receptor alpha (Ppara) and Ucp1 expression. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPARA | up-regulates quantity by expression
transcriptional regulation
|
AQP3 |
0.298 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255045 |
|
|
Homo sapiens |
Caki-1 Cell |
| pmid |
sentence |
| 17150915 |
To investigate the intimate function of PPARalpha in the kidney, we analyzed the target gene expression in human metastatic renal cell carcinoma cell line, Caki-1, using small interfering RNA (siRNA) against PPARalpha and real-time RT-PCR methods. We found that some selected genes (long-chain fatty-acid-CoA ligase (FACL1), carnitine palmitoyltransferase 1A (CPT1A), adipose differentiation-related protein (ADRP) and aquaporin 3 (AQP3)) were down-regulated by PPARalpha siRNA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPARA | up-regulates quantity by expression
transcriptional regulation
|
SLC25A20 |
0.491 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255049 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 19577614 |
CACT is upregulated by PPARalpha and PPARdelta, probably by binding to a functional PPRE at position +45 to +57 relative to the transcription start site. The upregulation of CACT by PPARalpha and PPARdelta, which are both important for the regulation of fatty acid oxidation in tissues during fasting, may increase the import of acylcarnitine into the mitochondrial matrix during fasting. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ARNTL | up-regulates quantity by expression
transcriptional regulation
|
PPARA |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268025 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 16556735 |
We demonstrate that PPARalpha plays a specific role in the peripheral circadian control because it is required to maintain the circadian rhythm of the master clock gene brain and muscle Arnt-like protein 1 (bmal1) in vivo. This regulation occurs via a direct binding of PPARalpha on a potential PPARalpha response element located in the bmal1 promoter. Reversely, BMAL1 is an upstream regulator of PPARalpha gene expression. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Liver |
| Pathways: | Circadian clock |
| + |
HUWE1 | down-regulates quantity by destabilization 
ubiquitination
|
PPARA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278814 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29331071 |
Furthermore, the E3 ubiquitin ligase HUWE1 was identified to mediate PPARalpha polyubiquitination.|This notion is also supported by our finding that Huwe1 knockdown up-regulated the expression of PPARalpha target genes at the cellular level. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RXRB | up-regulates
binding
|
PPARA |
0.565 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105448 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11237216 |
Although the three ppar subtypes are closely related and bind to similar dna response elements as heterodimers with the 9-cis retinoic acid receptor rxr, each subserves a distinct physiology |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TFEB | up-regulates quantity by expression
transcriptional regulation
|
PPARA |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276706 |
|
|
|
|
| pmid |
sentence |
| 33176151 |
Notably, TFEB regulates genes involved in several steps of lipid catabolism, which occur in different cellular compartments, such as the transport of fatty acid chains across the plasma membrane (for example, Cd36 and Fabps), and the β-oxidation of FFA in mitochondria (for example, Cpt1, Crat, Acadl, Acads and Hdad) and in peroxisomes (Cyp4a genes). |
|
| Publications: |
1 |
| + |
Gbeta | up-regulates activity
phosphorylation
|
PPARA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270079 |
|
|
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 10187842 |
We now demonstrate that amino acids 1-92 of hPPARalpha contain an activation function (AF)-1-like domain, which is further activated by insulin through a pathway involving the mitogen-activated protein kinases p42 and p44. Further analysis of the amino-terminal region of PPARalpha revealed that the insulin-induced trans-activation occurs through the phosphorylation of two mitogen-activated protein kinase sites at positions 12 and 21, both of which are conserved across evolution. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
dibutyl phthalate | up-regulates activity
chemical activation
|
PPARA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268748 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 33508418 |
Both in vitro and in vivo experiments have proved that DBP is a real activator of PPARα. he current study proves that plasticizer DBP has severe hepatotoxicity and could induce liver dysfunction even at normal doses after prolonged exposure. DBP might accumulate in the liver for a long time to activate PPARα/SREBP-1c/FAS/GPAT/AMPK and result in the accumulation of triglycerides and cholesterol in the liver. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
NR0B2 | up-regulates
binding
|
PPARA |
0.537 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-108252 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11369442 |
Surprisingly, shp potentiated transcription by pparalpha/rxralpha heterodimers from the hd-ppre. This is the first demonstration of positive transcriptional activity attributable to shp. Together, these results suggest that shp can modulate pparalpha/rxralpha-mediated transcription in a response element-specific manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPARA | up-regulates activity
|
LPL |
0.595 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251849 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16511610 |
The effect of fibrates on the metabolism of triglyceride-rich lipoproteins is due to a PPAR-alpha-dependent stimulation of lipoprotein lipase and of apolipoprotein (apo)A-V and to an inhibition of apoC-III expression, whereas the increase in plasma HDL-cholesterol depends partly on an overexpression of apoA-I and apoA-II. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
PPARA
- 
- 