| + |
EP300 | up-regulates quantity by expression 
transcriptional regulation
|
CPT1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254260 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 15199055 |
Furthermore, we show that the muscle carnitine palmitoyltransferase-1 and caveolin-3 promoters are directly regulated by ROR and coactivated by p300 and PGC-1. This study implicates RORs in the control of lipid homeostasis in skeletal muscle. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
RXRA | up-regulates quantity by expression
transcriptional regulation
|
CPT1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254582 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 15356291 |
Mutation analysis indicated that the MEF2 site contributed to the activation of the CPT1beta promoter by PPAR in C2C12 cells. The reporter construct containing the PPRE and the MEF2C site was synergistically activated by co-expression of PPAR, retinoid X receptor (RXR) and MEF2C in non-muscle cells. Moreover, protein-binding assays demonstrated that MEF2C and PPAR specifically bound to one another in vitro. Also for the synergistic activation of the CPT1beta gene promoter by MEF2C and PPARalpha-RXRalpha, a precise arrangement of its binding sites was essential. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
malonyl-CoA | down-regulates activity 
binding
|
CPT1B |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267115 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14517221 |
Carnitine palmitoyltransferase 1A (CPT1A) is the key regulatory enzyme of hepatic long-chain fatty acid beta-oxidation. The first component of this system is CPT1, an integral mitochondrial outer membrane protein, which catalyzes the transfer of long-chain acyl group of the acyl-CoA ester to carnitine. CPT1 is tightly regulated by its physiological inhibitor malonyl-CoA, the first intermediate in fatty acid biosynthesis. Three CPT1 isoforms with various tissue distribution and encoded by distinct genes have been identified (1., 2.): a liver (CPT1A or L-CPT1) (8.), a muscle (CPT1B or M-CPT1) (9.), and a brain isoform (CPT1C). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPARGC1A | up-regulates quantity by expression
transcriptional regulation
|
CPT1B |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254262 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 15199055 |
Furthermore, we show that the muscle carnitine palmitoyltransferase-1 and caveolin-3 promoters are directly regulated by ROR and coactivated by p300 and PGC-1. This study implicates RORs in the control of lipid homeostasis in skeletal muscle. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PPARG | up-regulates quantity by expression
transcriptional regulation
|
CPT1B |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254581 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 15356291 |
Mutation analysis indicated that the MEF2 site contributed to the activation of the CPT1beta promoter by PPAR in C2C12 cells. The reporter construct containing the PPRE and the MEF2C site was synergistically activated by co-expression of PPAR, retinoid X receptor (RXR) and MEF2C in non-muscle cells. Moreover, protein-binding assays demonstrated that MEF2C and PPAR specifically bound to one another in vitro. Also for the synergistic activation of the CPT1beta gene promoter by MEF2C and PPARalpha-RXRalpha, a precise arrangement of its binding sites was essential. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CPT1B | up-regulates quantity 
chemical modification
|
coenzyme A(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267133 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14517221 |
Carnitine palmitoyltransferase 1A (CPT1A) is the key regulatory enzyme of hepatic long-chain fatty acid beta-oxidation. The first component of this system is CPT1, an integral mitochondrial outer membrane protein, which catalyzes the transfer of long-chain acyl group of the acyl-CoA ester to carnitine. CPT1 is tightly regulated by its physiological inhibitor malonyl-CoA, the first intermediate in fatty acid biosynthesis. Three CPT1 isoforms with various tissue distribution and encoded by distinct genes have been identified (1., 2.): a liver (CPT1A or L-CPT1) (8.), a muscle (CPT1B or M-CPT1) (9.), and a brain isoform (CPT1C). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CPT1B | up-regulates quantity
chemical modification
|
O-palmitoyl-L-carnitine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267130 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14517221 |
Carnitine palmitoyltransferase 1A (CPT1A) is the key regulatory enzyme of hepatic long-chain fatty acid beta-oxidation. The first component of this system is CPT1, an integral mitochondrial outer membrane protein, which catalyzes the transfer of long-chain acyl group of the acyl-CoA ester to carnitine. CPT1 is tightly regulated by its physiological inhibitor malonyl-CoA, the first intermediate in fatty acid biosynthesis. Three CPT1 isoforms with various tissue distribution and encoded by distinct genes have been identified (1., 2.): a liver (CPT1A or L-CPT1) (8.), a muscle (CPT1B or M-CPT1) (9.), and a brain isoform (CPT1C). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MEF2C | up-regulates quantity by expression
transcriptional regulation
|
CPT1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254583 |
|
|
Mus musculus |
Adenocarcinoma Cell Line |
| pmid |
sentence |
| 15356291 |
Mutation analysis indicated that the MEF2 site contributed to the activation of the CPT1beta promoter by PPAR in C2C12 cells. The reporter construct containing the PPRE and the MEF2C site was synergistically activated by co-expression of PPAR, retinoid X receptor (RXR) and MEF2C in non-muscle cells. Moreover, protein-binding assays demonstrated that MEF2C and PPAR specifically bound to one another in vitro. Also for the synergistic activation of the CPT1beta gene promoter by MEF2C and PPARalpha-RXRalpha, a precise arrangement of its binding sites was essential. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RORA | up-regulates quantity by expression
transcriptional regulation
|
CPT1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254256 |
|
|
Mus musculus |
Skeletal Muscle |
| pmid |
sentence |
| 15199055 |
Furthermore, we show that the muscle carnitine palmitoyltransferase-1 and caveolin-3 promoters are directly regulated by ROR and coactivated by p300 and PGC-1. This study implicates RORs in the control of lipid homeostasis in skeletal muscle. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CPT1B | down-regulates quantity
chemical modification
|
(R)-carnitine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267121 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14517221 |
Carnitine palmitoyltransferase 1A (CPT1A) is the key regulatory enzyme of hepatic long-chain fatty acid beta-oxidation. The first component of this system is CPT1, an integral mitochondrial outer membrane protein, which catalyzes the transfer of long-chain acyl group of the acyl-CoA ester to carnitine. CPT1 is tightly regulated by its physiological inhibitor malonyl-CoA, the first intermediate in fatty acid biosynthesis. Three CPT1 isoforms with various tissue distribution and encoded by distinct genes have been identified (1., 2.): a liver (CPT1A or L-CPT1) (8.), a muscle (CPT1B or M-CPT1) (9.), and a brain isoform (CPT1C). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CPT1B | down-regulates quantity
chemical modification
|
palmitoyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267127 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14517221 |
Carnitine palmitoyltransferase 1A (CPT1A) is the key regulatory enzyme of hepatic long-chain fatty acid beta-oxidation. The first component of this system is CPT1, an integral mitochondrial outer membrane protein, which catalyzes the transfer of long-chain acyl group of the acyl-CoA ester to carnitine. CPT1 is tightly regulated by its physiological inhibitor malonyl-CoA, the first intermediate in fatty acid biosynthesis. Three CPT1 isoforms with various tissue distribution and encoded by distinct genes have been identified (1., 2.): a liver (CPT1A or L-CPT1) (8.), a muscle (CPT1B or M-CPT1) (9.), and a brain isoform (CPT1C). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CPT1B
- 
- 