| + |
CEBPB | up-regulates quantity by expression 
transcriptional regulation
|
GOT1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254051 |
|
|
|
|
| pmid |
sentence |
| 8454627 |
In cotransfection experiments, the C/EBP beta protein trans-activated 10-15-fold the cAspAT gene promoter in HepG2 cells. Deletion studies revealed that regions P2 and P4 are critical for promoter activity. In gel retardation experiments, the P4 region bound different C/EBP-related proteins in different tissues |
|
| Publications: |
1 |
| + |
GOT1 | down-regulates quantity 
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268064 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26003525 |
Glutamate oxaloacetate transaminase (GOT) catalyzes the reversible reaction of l-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate and plays a key role in carbon and nitrogen metabolism in all organisms. In human tissues, GOTs are pyridoxal 5'-phosphate-dependent (PLP) enzymes which exist in cytoplasm and mitochondrial forms, GOT1 and GOT2, respectively. GOT1 expression correlates with the growth of several tumors because cancer cells can utilize the amino acid glutamine to fuel anabolic processes, and therefore, GOT1 represents a new therapeutic target in cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
GOT1 | down-regulates quantity
chemical modification
|
oxaloacetate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268061 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26003525 |
Glutamate oxaloacetate transaminase (GOT) catalyzes the reversible reaction of l-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate and plays a key role in carbon and nitrogen metabolism in all organisms. In human tissues, GOTs are pyridoxal 5'-phosphate-dependent (PLP) enzymes which exist in cytoplasm and mitochondrial forms, GOT1 and GOT2, respectively. GOT1 expression correlates with the growth of several tumors because cancer cells can utilize the amino acid glutamine to fuel anabolic processes, and therefore, GOT1 represents a new therapeutic target in cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
GOT1 | down-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268063 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26003525 |
Glutamate oxaloacetate transaminase (GOT) catalyzes the reversible reaction of l-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate and plays a key role in carbon and nitrogen metabolism in all organisms. In human tissues, GOTs are pyridoxal 5'-phosphate-dependent (PLP) enzymes which exist in cytoplasm and mitochondrial forms, GOT1 and GOT2, respectively. GOT1 expression correlates with the growth of several tumors because cancer cells can utilize the amino acid glutamine to fuel anabolic processes, and therefore, GOT1 represents a new therapeutic target in cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism |
| + |
GOT1 | up-regulates quantity
chemical modification
|
2-oxoglutarate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267505 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26003525 |
Glutamate oxaloacetate transaminase (GOT) catalyzes the reversible reaction of l-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate and plays a key role in carbon and nitrogen metabolism in all organisms. In human tissues, GOTs are pyridoxal 5'-phosphate-dependent (PLP) enzymes which exist in cytoplasm and mitochondrial forms, GOT1 and GOT2, respectively. GOT1 expression correlates with the growth of several tumors because cancer cells can utilize the amino acid glutamine to fuel anabolic processes, and therefore, GOT1 represents a new therapeutic target in cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism |
| + |
GOT1 | up-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267506 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26003525 |
Glutamate oxaloacetate transaminase (GOT) catalyzes the reversible reaction of l-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate and plays a key role in carbon and nitrogen metabolism in all organisms. In human tissues, GOTs are pyridoxal 5'-phosphate-dependent (PLP) enzymes which exist in cytoplasm and mitochondrial forms, GOT1 and GOT2, respectively. GOT1 expression correlates with the growth of several tumors because cancer cells can utilize the amino acid glutamine to fuel anabolic processes, and therefore, GOT1 represents a new therapeutic target in cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
GOT1 | down-regulates quantity
chemical modification
|
2-oxoglutarate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268062 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26003525 |
Glutamate oxaloacetate transaminase (GOT) catalyzes the reversible reaction of l-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate and plays a key role in carbon and nitrogen metabolism in all organisms. In human tissues, GOTs are pyridoxal 5'-phosphate-dependent (PLP) enzymes which exist in cytoplasm and mitochondrial forms, GOT1 and GOT2, respectively. GOT1 expression correlates with the growth of several tumors because cancer cells can utilize the amino acid glutamine to fuel anabolic processes, and therefore, GOT1 represents a new therapeutic target in cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism |
| + |
GOT1 | up-regulates quantity
chemical modification
|
oxaloacetate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267509 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26003525 |
Glutamate oxaloacetate transaminase (GOT) catalyzes the reversible reaction of l-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate and plays a key role in carbon and nitrogen metabolism in all organisms. In human tissues, GOTs are pyridoxal 5'-phosphate-dependent (PLP) enzymes which exist in cytoplasm and mitochondrial forms, GOT1 and GOT2, respectively. GOT1 expression correlates with the growth of several tumors because cancer cells can utilize the amino acid glutamine to fuel anabolic processes, and therefore, GOT1 represents a new therapeutic target in cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
GOT1 | up-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267510 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26003525 |
Glutamate oxaloacetate transaminase (GOT) catalyzes the reversible reaction of l-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate and plays a key role in carbon and nitrogen metabolism in all organisms. In human tissues, GOTs are pyridoxal 5'-phosphate-dependent (PLP) enzymes which exist in cytoplasm and mitochondrial forms, GOT1 and GOT2, respectively. GOT1 expression correlates with the growth of several tumors because cancer cells can utilize the amino acid glutamine to fuel anabolic processes, and therefore, GOT1 represents a new therapeutic target in cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism |
3.0
GOT1
- 
- 