| + |
GSK3B | up-regulates activity 
phosphorylation
|
ACLY |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251218 |
Ser451 |
STSTPAPsRTASFSE |
|
|
| pmid |
sentence |
| 10653665 |
Thr 446 and Ser 450, which are phosphorylated by glycogen synthase kinase-3 (GSK-3) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251219 |
Thr447 |
NASGSTStPAPSRTA |
|
|
| pmid |
sentence |
| 10653665 |
Thr 446 and Ser 450, which are phosphorylated by glycogen synthase kinase-3 (GSK-3). Phosphorylation resulted in a 6-fold increase in V(max) and the conversion of citrate dependence from sigmoidal, displaying negative cooperativity, to hyperbolic. |
|
| Publications: |
2 |
| + |
PRKACA | up-regulates activity
phosphorylation
|
ACLY |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250328 |
Ser455 |
PAPSRTAsFSESRAD |
in vitro |
|
| pmid |
sentence |
| 10653665 |
Phosphorylation of Recombinant Human ATP:Citrate Lyase by cAMP-Dependent Protein Kinase Abolishes Homotropic Allosteric Regulation of the Enzyme by Citrate and Increases the Enzyme Activity. Ser 454, which is phosphorylated by the catalytic subunit of cAMP-dependent protein kinase (PKA) |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AKT2 |
phosphorylation
|
ACLY |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245263 |
Ser455 |
PAPSRTAsFSESRAD |
Rattus norvegicus |
Adipocyte |
| pmid |
sentence |
| 12107176 |
Taken together, these results demonstrate that serine 454 of ATP-citrate lyase is a novel and major in vivo substrate for protein kinase B. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
AKT1 |
phosphorylation
|
ACLY |
0.446 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245255 |
Ser455 |
PAPSRTAsFSESRAD |
Rattus norvegicus |
Adipocyte |
| pmid |
sentence |
| 12107176 |
Taken together, these results demonstrate that serine 454 of ATP-citrate lyase is a novel and major in vivo substrate for protein kinase B. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
AKT |
phosphorylation
|
ACLY |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245259 |
Ser455 |
PAPSRTAsFSESRAD |
Rattus norvegicus |
Adipocyte |
| pmid |
sentence |
| 12107176 |
Taken together, these results demonstrate that serine 454 of ATP-citrate lyase is a novel and major in vivo substrate for protein kinase B. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
SRC | up-regulates activity
phosphorylation
|
ACLY |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274107 |
Tyr1006 |
PATPLLDyALEVEKI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32420483 |
We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274108 |
Tyr227 |
KVDATADyICKVKWG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32420483 |
We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274109 |
Tyr252 |
EAYPEEAyIADLDAK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32420483 |
We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274106 |
Tyr682 |
SRTTDGVyEGVAIGG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32420483 |
We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
ACLY |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274104 |
Tyr227 |
KVDATADyICKVKWG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32420483 |
We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274105 |
Tyr252 |
EAYPEEAyIADLDAK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32420483 |
We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274103 |
Tyr682 |
SRTTDGVyEGVAIGG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32420483 |
We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
SREBF1 | up-regulates quantity by expression 
transcriptional regulation
|
ACLY |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267956 |
|
|
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 |
| + |
ACLY | down-regulates quantity by destabilization 
chemical modification
|
citrate(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267101 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19286649 |
ATP citrate lyase (ACL) is a cytosolic enzyme that catalyzes the synthesis of acetyl-CoA and oxaloacetate using citrate, CoA, and ATP as substrates and Mg(2+) as a necessary cofactor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Citric acid cycle, Fatty Acid Synthesis |
| + |
ACLY | up-regulates quantity
chemical modification
|
oxaloacetate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267102 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19286649 |
ATP citrate lyase (ACL) is a cytosolic enzyme that catalyzes the synthesis of acetyl-CoA and oxaloacetate using citrate, CoA, and ATP as substrates and Mg(2+) as a necessary cofactor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Citric acid cycle, Fatty Acid Synthesis |
| + |
ACLY | up-regulates quantity
chemical modification
|
acetyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267103 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19286649 |
ATP citrate lyase (ACL) is a cytosolic enzyme that catalyzes the synthesis of acetyl-CoA and oxaloacetate using citrate, CoA, and ATP as substrates and Mg(2+) as a necessary cofactor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Citric acid cycle, Fatty Acid Synthesis |
| + |
ACLY | down-regulates quantity by destabilization
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268082 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19286649 |
ATP citrate lyase (ACL) is a cytosolic enzyme that catalyzes the synthesis of acetyl-CoA and oxaloacetate using citrate, CoA, and ATP as substrates and Mg(2+) as a necessary cofactor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KLHL25 | down-regulates quantity by destabilization
binding
|
ACLY |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272333 |
|
|
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 27664236 |
Here, we found that CUL3 interacts with ACLY through its adaptor protein, KLHL25 (Kelch-like family member 25), to ubiquitinate and degrade ACLY in cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACLY | down-regulates quantity by destabilization
chemical modification
|
coenzyme A(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268081 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19286649 |
ATP citrate lyase (ACL) is a cytosolic enzyme that catalyzes the synthesis of acetyl-CoA and oxaloacetate using citrate, CoA, and ATP as substrates and Mg(2+) as a necessary cofactor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACLY | up-regulates quantity
chemical modification
|
ADP(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268080 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19286649 |
ATP citrate lyase (ACL) is a cytosolic enzyme that catalyzes the synthesis of acetyl-CoA and oxaloacetate using citrate, CoA, and ATP as substrates and Mg(2+) as a necessary cofactor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Cullin 3-RBX1-Skp1 | down-regulates quantity by destabilization
binding
|
ACLY |
0.291 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272335 |
|
|
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 27664236 |
Here, we found that CUL3 interacts with ACLY through its adaptor protein, KLHL25 (Kelch-like family member 25), to ubiquitinate and degrade ACLY in cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ACLY
- 
- 