| + |
FASN | up-regulates quantity by stabilization 
|
CTNNB1 |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242878 |
|
|
Homo sapiens |
Prostate Gland Cancer Cell |
| pmid |
sentence |
| 18838960 |
Overexpression of fatty acid synthase is associated with palmitoylation of Wnt1 and cytoplasmic stabilization of beta-catenin in prostate cancer |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HACD4 | up-regulates activity 
chemical activation
|
FASN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267763 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18554506 |
Very long-chain fatty acids are produced through a four-step cycle. However, the 3-hydroxyacyl-CoA dehydratase catalyzing the third step in mammals has remained unidentified. Mammals have four candidates, HACD1-4, based on sequence similarities to the recently identified yeast Phs1, although HACD3 and HACD4 share relatively weak similarity. We demonstrate that all four of these human proteins are indeed 3-hydroxyacyl-CoA dehydratases, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FASN | up-regulates quantity
chemical modification
|
hexadecanoic acid |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267373 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12689621 |
An organizational model for animal FAS was proposed in which the two subunits depicted in domains I, II, and III were arranged in an antiparallel fashion, thereby generating two sites for palmitate synthesis. Initiation of the series of condensation reactions leading to the production of palmitic acid requires the translocation of one acetyl and seven malonyl moieties, from CoA thioester to the phosphopantetheine thiol of the ACP domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
| + |
NADPH(4-) | up-regulates activity
binding
|
FASN |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267371 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34765544 |
We determined that FASN inhibitor treatment resulted in NADPH accumulation and inhibition of PGDH enzyme activity. NADPH is a cofactor utilized by FASN, also a known allosteric inhibitor of PGDH. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
| + |
TRIM21 | down-regulates quantity by destabilization 
ubiquitination
|
FASN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267368 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27758890 |
FASN acetylation enhanced its association with the E3 ubiquitin ligase TRIM21. Acetylation destabilized FASN and resulted in decreased de novo lipogenesis and tumor cell growth. FASN acetylation was frequently reduced in human hepatocellular carcinoma samples, which correlated with increased HDAC3 expression and FASN protein levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SREBF1 | up-regulates quantity by expression
transcriptional regulation
|
FASN |
0.511 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242884 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20373869 |
Ultimately, both the AKT and MAPK transduction pathways regulate FASN expression through the modulation of expression of sterol regulatory element-binding protein (SREBP)-1c, which binds to regulatory elements in the FASN promoter. Proto-oncogene FBI-1 (Pokemon), a transcription factor of the bric--brac tramtrack broad complex/pox viruses and zinc fingers (BTB/POZ) domain family, interacts directly with SREBP-1c through its DNA-binding domain to synergistically activate the transcription of FASN |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142294 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16308421 |
Well-described targets of srebp-1 and the carbohydrate response element binding protein (chrebp), which include the following: fatty acid synthase (fas), acetyl coa carboxylase (acc1), and liver pyruvate kinase (l-pk) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Circadian clock |
| + |
KAT8 | down-regulates quantity by destabilization
acetylation
|
FASN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267366 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27758890 |
Overexpression of Myc-KAT8 increased the acetylation level of endogenous FASN by 2.2-fold (Fig. 3C). In contrast, knockdown of KAT8 decreased endogenous FASN acetylation by as much as 55% |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HACD1 | up-regulates activity
chemical activation
|
FASN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267760 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18554506 |
Very long-chain fatty acids are produced through a four-step cycle. However, the 3-hydroxyacyl-CoA dehydratase catalyzing the third step in mammals has remained unidentified. Mammals have four candidates, HACD1-4, based on sequence similarities to the recently identified yeast Phs1, although HACD3 and HACD4 share relatively weak similarity. We demonstrate that all four of these human proteins are indeed 3-hydroxyacyl-CoA dehydratases, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FASN | down-regulates quantity
chemical modification
|
NADPH(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267759 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15507492 |
Human fatty acid synthase (FAS) is a complex homodimeric (552-kDa) enzyme that regulates the de novo biosynthesis of long-chain fatty acids. This cytosolic enzyme catalyzes the formation of 16 carbon (C16) palmitate, from acetyl-coenzyme A (acetyl-CoA) and malonyl-coenzyme A (malonyl-CoA) in the presence of NADPH.  |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
| + |
HACD | up-regulates activity
chemical activation
|
FASN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267764 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18554506 |
Very long-chain fatty acids are produced through a four-step cycle. However, the 3-hydroxyacyl-CoA dehydratase catalyzing the third step in mammals has remained unidentified. Mammals have four candidates, HACD1-4, based on sequence similarities to the recently identified yeast Phs1, although HACD3 and HACD4 share relatively weak similarity. We demonstrate that all four of these human proteins are indeed 3-hydroxyacyl-CoA dehydratases, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
| + |
HDAC3 | up-regulates quantity by stabilization
deacetylation
|
FASN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267367 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27758890 |
Overexpression of HA-HDAC3 decreased the acetylation level of endogenous FASN by 35% in HEK293T cells, while the expression of a catalytic inactive mutant HDAC3Y298H (38) failed to reduce FASN acetylation (Fig. 4C). Conversely, HDAC3 knockdown increased the acetylation level of endogenous FASN by >1.5-fold in HEK293T cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FASN | up-regulates quantity
chemical modification
|
NADP(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268087 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15507492 |
Human fatty acid synthase (FAS) is a complex homodimeric (552-kDa) enzyme that regulates the de novo biosynthesis of long-chain fatty acids. This cytosolic enzyme catalyzes the formation of 16 carbon (C16) palmitate, from acetyl-coenzyme A (acetyl-CoA) and malonyl-coenzyme A (malonyl-CoA) in the presence of NADPH.  |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HACD2 | up-regulates activity
chemical activation
|
FASN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267761 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18554506 |
Very long-chain fatty acids are produced through a four-step cycle. However, the 3-hydroxyacyl-CoA dehydratase catalyzing the third step in mammals has remained unidentified. Mammals have four candidates, HACD1-4, based on sequence similarities to the recently identified yeast Phs1, although HACD3 and HACD4 share relatively weak similarity. We demonstrate that all four of these human proteins are indeed 3-hydroxyacyl-CoA dehydratases, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HACD3 | up-regulates activity
chemical activation
|
FASN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267762 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18554506 |
Very long-chain fatty acids are produced through a four-step cycle. However, the 3-hydroxyacyl-CoA dehydratase catalyzing the third step in mammals has remained unidentified. Mammals have four candidates, HACD1-4, based on sequence similarities to the recently identified yeast Phs1, although HACD3 and HACD4 share relatively weak similarity. We demonstrate that all four of these human proteins are indeed 3-hydroxyacyl-CoA dehydratases, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FASN | up-regulates
|
Lipogenesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242874 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20373869 |
Fatty acid synthase (FASN) is a key enzyme involved in neoplastic lipogenesis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FASN | down-regulates quantity
chemical modification
|
malonyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267212 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15507492 |
Human fatty acid synthase (FAS) is a complex homodimeric (552-kDa) enzyme that regulates the de novo biosynthesis of long-chain fatty acids. This cytosolic enzyme catalyzes the formation of 16 carbon (C16) palmitate, from acetyl-coenzyme A (acetyl-CoA) and malonyl-coenzyme A (malonyl-CoA) in the presence of NADPH.  |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
| + |
FASN | up-regulates quantity
chemical modification
|
coenzyme A(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268086 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15507492 |
Human fatty acid synthase (FAS) is a complex homodimeric (552-kDa) enzyme that regulates the de novo biosynthesis of long-chain fatty acids. This cytosolic enzyme catalyzes the formation of 16 carbon (C16) palmitate, from acetyl-coenzyme A (acetyl-CoA) and malonyl-coenzyme A (malonyl-CoA) in the presence of NADPH.  |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FASN | up-regulates quantity
chemical modification
|
long-chain fatty acid anion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267208 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15507492 |
Human fatty acid synthase (FAS) is a complex homodimeric (552-kDa) enzyme that regulates the de novo biosynthesis of long-chain fatty acids. This cytosolic enzyme catalyzes the formation of 16 carbon (C16) palmitate, from acetyl-coenzyme A (acetyl-CoA) and malonyl-coenzyme A (malonyl-CoA) in the presence of NADPH.  |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
| + |
FASN | up-regulates
|
Fatty_Acid_Biosynthesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270536 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9356448 |
Our model of the native fatty acid synthase (FAS) depicts it as a dimer of two identical multifunctional proteins (Mr approximately 272,000) arranged in an antiparallel configuration so that the active Cys-SH of the beta-ketoacyl synthase of one subunit (where the acyl group is attached) is juxtaposed within 2 A of the pantetheinyl-SH of the second subunit (where the malonyl group is bound). This arrangement generates two active centers for fatty acid synthesis and predicts that if we have two appropriate halves of the monomer, we should be able to reconstitute an active fatty acid-synthesizing site |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268159 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9356448 |
Our model of the native fatty acid synthase (FAS) depicts it as a dimer of two identical multifunctional proteins (Mr approximately 272,000) arranged in an antiparallel configuration so that the active Cys-SH of the beta-ketoacyl synthase of one subunit (where the acyl group is attached) is juxtaposed within 2 A of the pantetheinyl-SH of the second subunit (where the malonyl group is bound). This arrangement generates two active centers for fatty acid synthesis and predicts that if we have two appropriate halves of the monomer, we should be able to reconstitute an active fatty acid-synthesizing site |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Circadian clock |
| + |
FASN | up-regulates activity
|
WNT1 |
0.252 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242881 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18838960 |
Overexpression of fatty acid synthase is associated with palmitoylation of Wnt1 and cytoplasmic stabilization of beta-catenin in prostate cancer |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FASN | down-regulates quantity
chemical modification
|
acetyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267211 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15507492 |
Human fatty acid synthase (FAS) is a complex homodimeric (552-kDa) enzyme that regulates the de novo biosynthesis of long-chain fatty acids. This cytosolic enzyme catalyzes the formation of 16 carbon (C16) palmitate, from acetyl-coenzyme A (acetyl-CoA) and malonyl-coenzyme A (malonyl-CoA) in the presence of NADPH.  |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
3.0
FASN
- 
- 