| + |
PRKAA1 | down-regulates activity 
phosphorylation
|
ACACA |
0.702 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250400 |
Ser1201 |
IPTLNRMsFSSNLNH |
Rattus norvegicus |
|
| pmid |
sentence |
| 7907095 |
We have isolated and purified from rat livers a novel kinase that phosphorylates and inactivates the carboxylase Ser1200 isphosphorylated by both CAMP-dependent protein kinase and AMP-activated protein kinase |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKACA | down-regulates activity
phosphorylation
|
ACACA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267714 |
Ser1201 |
IPTLNRMsFSSNLNH |
in vitro |
|
| pmid |
sentence |
| 2900138 |
TC1 = Ser-2Ser(P)-Met-3Ser(P)-Gly-Leu; TC2 = Arg-Met-1Ser(P)-Phe- Cyclic-AMP-dependent protein kinase phosphorylates sites 1 and 2 exclusively, whereas the AMP-activated protein kinase phosphorylates sites 1 and 3, plus at least one other minor site.[…]The results suggest that phosphorylation of site 3 is primarily responsible for the large decrease in Vmax produced by the AMP-activated protein kinase, while phosphorylation of site 1 may be primarily responsible for the increase in A0.5 for citrate and more modest depression of Vmax produced by cyclic-AMP-dependent protein kinase and ACK2 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CSNK2A1 |
phosphorylation
|
ACACA |
0.305 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250823 |
Ser29 |
GSVSEDNsEDEISNL |
in vitro |
|
| pmid |
sentence |
| 2900140 |
These results show that casein kinase-2 phosphorylates site 6 exclusively |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CSNK2A2 |
phosphorylation
|
ACACA |
0.305 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250973 |
Ser29 |
GSVSEDNsEDEISNL |
in vitro |
|
| pmid |
sentence |
| 2900140 |
Phosphorylation at site 6 by casein kinase-2 is in good agreement with previous studies on the specificity of this kinase, which is known to phosphorylate serine residues followed by an acidic cluster |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPP4C | up-regulates activity 
dephosphorylation
|
ACACA |
0.241 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267724 |
Ser80 |
LHIRSSMsGLHLVKQ |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 25050742 |
PP4 was also found to directly interact with pACC1‑Ser79 in human HepG2 cells. In conclusion, the present study showed that PP4 may be a novel regulator in hepatic lipogenesis through dephosphorylating ACC1 on serine 79, suggesting that PP4 may be a promising therapeutic target in lipid metabolism disorders. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMPK | down-regulates activity
phosphorylation
|
ACACA |
0.561 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267475 |
Ser80 |
LHIRSSMsGLHLVKQ |
Homo sapiens |
|
| pmid |
sentence |
| 29899443 |
Human ACC1 is inactivated by phosphorylation at Ser80, Ser1201 and Ser1216 by AMP-activated protein kinase (AMPK) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Leptin Signaling |
| + |
AMPK | down-regulates
phosphorylation
|
ACACA |
0.561 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216655 |
Ser80 |
LHIRSSMsGLHLVKQ |
Homo sapiens |
|
| pmid |
sentence |
| 12015362 |
Significant negative linear correlations between phospho-acc and acc activity were observed in all models (p < 0.01). The decline in acc activity was related to the decrease in pcr and the rise in amp. A relationship between phospho-ampk (threonine 172) and activity of ampk immunoprecipitated with anti-alpha(2) subunit antibody preparation was also observed. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| Pathways: | Leptin Signaling |
| + |
PRKAA2 | down-regulates
phosphorylation
|
ACACA |
0.699 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87583 |
Ser80 |
LHIRSSMsGLHLVKQ |
Homo sapiens |
|
| pmid |
sentence |
| 12015362 |
Significant negative linear correlations between phospho-acc and acc activity were observed in all models (p < 0.01). The decline in acc activity was related to the decrease in pcr and the rise in amp. A relationship between phospho-ampk (threonine 172) and activity of ampk immunoprecipitated with anti-alpha(2) subunit antibody preparation was also observed. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
ACACA | down-regulates 
|
Food intake |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263509 |
|
|
Homo sapiens |
Pulmonary Artery Smooth Muscle Cell |
| pmid |
sentence |
| 25343030 |
Leptin exerts an inhibitory effect on AMPK in the hypothalamus, thereby stimulating ACC and subsequently suppressing food intake. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Leptin Signaling |
| + |
MLXIPL | up-regulates quantity by expression
transcriptional regulation
|
ACACA |
0.436 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267946 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 15496471 |
The present study provides evidence for a direct and dominant role of ChREBP in the glucose regulation of two key liver lipogenic enzymes, acetyl-CoA carboxylase (ACC) and fatty acid synthase (FAS) |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Liver |
| + |
ACACA | down-regulates quantity
chemical modification
|
acetyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267105 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20952656 |
ACC catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting and first committed step in de novo fatty acid biosynthesis. Two isoforms of ACC exist in mammals, ACC1 and ACC2, and both enzymes function to carboxylate acetyl-CoA to form malonyl-CoA |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
| + |
COP1 | down-regulates quantity by destabilization
ubiquitination
|
ACACA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271598 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16794074 |
TRB3 appears to inhibit ACC activity by functioning as an adaptor for COP1. Taken together, these results suggest that TRB3 may promote loss of fat by mediating the COP1-dependent ubiquitination and inactivation of ACC. Taking these results together, we propose that TRB3 may protect against diet-induced obesity by stimulating fatty acid oxidation in adipose during fasting through the COP1-mediated ubiquitination and degradation of ACC (Fig. 4D). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRIB3 | down-regulates quantity by destabilization
binding
|
ACACA |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271600 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16794074 |
TRB3 appears to inhibit ACC activity by functioning as an adaptor for COP1. Taken together, these results suggest that TRB3 may promote loss of fat by mediating the COP1-dependent ubiquitination and inactivation of ACC. Taking these results together, we propose that TRB3 may protect against diet-induced obesity by stimulating fatty acid oxidation in adipose during fasting through the COP1-mediated ubiquitination and degradation of ACC (Fig. 4D). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACACA | up-regulates quantity
chemical modification
|
malonyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267109 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20952656 |
ACC catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting and first committed step in de novo fatty acid biosynthesis. Two isoforms of ACC exist in mammals, ACC1 and ACC2, and both enzymes function to carboxylate acetyl-CoA to form malonyl-CoA |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
| + |
SREBF1 | up-regulates quantity by expression 
transcriptional regulation
|
ACACA |
0.457 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267957 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11994399 |
SREBP-1c–responsive genes include those for ATP citrate lyase (which produces acetyl-CoA) and acetyl-CoA carboxylase and fatty acid synthase (which together produce palmitate [C16:0]). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
citrate(3-) | up-regulates activity
binding
|
ACACA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267104 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 6138356 |
Citrate, an allosteric activator of acetyl-CoA carboxylase, induces polymerization of an inactive protomeric form of the enzyme into an active filamentous form composed of 10-20 protomers. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
| + |
BRCA1 | down-regulates activity
binding
|
ACACA |
0.545 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267474 |
|
|
in vitro |
|
| pmid |
sentence |
| 16698035 |
ACCA binds BRCA1 when phosphorylated onSer1263, thus supporting a model in which controlof lipid synthesis would be mediated at least in part,viaphosphorylation of the Ser1263. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MID1IP1 | up-regulates activity
binding
|
ACACA |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267111 |
|
|
Cricetulus griseus |
CHO-K1 Cell |
| pmid |
sentence |
| 20952656 |
Recently, we reported the discovery that MIG12, a 183 amino acid protein, binds to ACC1 and ACC2, which induces polymerization and subsequently increases the enzymatic activity of the protein |
|
| Publications: |
1 |
Organism: |
Cricetulus Griseus |
4.0
ACACA
- 
- 