| + |
ULK2 | down-regulates activity 
phosphorylation
|
ENO1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274038 |
Ser115 |
ANAILGVsLAVCKAG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27153534 |
Here, we demonstrate that, during deprivation of amino acid and growth factors, ULK1/2 directly phosphorylate key glycolytic enzymes including hexokinase (HK), phosphofructokinase 1 (PFK1), enolase 1 (ENO1), and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBP1).Phosphorylation of these enzymes leads to enhanced HK activity to sustain glucose uptake but reduced activity of FBP1 to block the gluconeogenic route and reduced activity of PFK1 and ENO1 to moderate drop of glucose-6-phosphate and to repartition more carbon flux to pentose phosphate pathway (PPP), maintaining cellular energy and redox homeostasis at cellular and organismal levels.Similar results were also obtained using ULK2 as the kinase (data not shown). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274037 |
Ser282 |
QLADLYKsFIKDYPV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27153534 |
Here, we demonstrate that, during deprivation of amino acid and growth factors, ULK1/2 directly phosphorylate key glycolytic enzymes including hexokinase (HK), phosphofructokinase 1 (PFK1), enolase 1 (ENO1), and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBP1).Phosphorylation of these enzymes leads to enhanced HK activity to sustain glucose uptake but reduced activity of FBP1 to block the gluconeogenic route and reduced activity of PFK1 and ENO1 to moderate drop of glucose-6-phosphate and to repartition more carbon flux to pentose phosphate pathway (PPP), maintaining cellular energy and redox homeostasis at cellular and organismal levels.Similar results were also obtained using ULK2 as the kinase (data not shown). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ULK2 | up-regulates activity 
phosphorylation
|
HK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274042 |
Ser124 |
NIVHGSGsQLFDHVA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27153534 |
Here, we demonstrate that, during deprivation of amino acid and growth factors, ULK1/2 directly phosphorylate key glycolytic enzymes including hexokinase (HK), phosphofructokinase 1 (PFK1), enolase 1 (ENO1), and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBP1).Phosphorylation of these enzymes leads to enhanced HK activity to sustain glucose uptake but reduced activity of FBP1 to block the gluconeogenic route and reduced activity of PFK1 and ENO1 to moderate drop of glucose-6-phosphate and to repartition more carbon flux to pentose phosphate pathway (PPP), maintaining cellular energy and redox homeostasis at cellular and organismal levels.Similar results were also obtained using ULK2 as the kinase (data not shown). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274041 |
Ser364 |
TRLGVEPsDDDCVSV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27153534 |
Here, we demonstrate that, during deprivation of amino acid and growth factors, ULK1/2 directly phosphorylate key glycolytic enzymes including hexokinase (HK), phosphofructokinase 1 (PFK1), enolase 1 (ENO1), and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBP1).Phosphorylation of these enzymes leads to enhanced HK activity to sustain glucose uptake but reduced activity of FBP1 to block the gluconeogenic route and reduced activity of PFK1 and ENO1 to moderate drop of glucose-6-phosphate and to repartition more carbon flux to pentose phosphate pathway (PPP), maintaining cellular energy and redox homeostasis at cellular and organismal levels.Similar results were also obtained using ULK2 as the kinase (data not shown). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ULK2 | up-regulates activity
phosphorylation
|
DENND3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264732 |
Ser472 |
THRRMVVsMPNLQDI |
Homo sapiens |
|
| pmid |
sentence |
| 25925668 |
ULK-mediated phosphorylation of the guanine nucleotide exchange factor DENND3 at serines 554 and 572 upregulates its GEF activity toward the small GTPase Rab12. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264733 |
Ser490 |
ELAPRNSsLRLTDTA |
Homo sapiens |
|
| pmid |
sentence |
| 25925668 |
ULK-mediated phosphorylation of the guanine nucleotide exchange factor DENND3 at serines 554 and 572 upregulates its GEF activity toward the small GTPase Rab12. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ULK2 | down-regulates activity
phosphorylation
|
FBP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274040 |
Ser63 |
HLYGIAGsTNVTGDQ |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27153534 |
Here, we demonstrate that, during deprivation of amino acid and growth factors, ULK1/2 directly phosphorylate key glycolytic enzymes including hexokinase (HK), phosphofructokinase 1 (PFK1), enolase 1 (ENO1), and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBP1).Phosphorylation of these enzymes leads to enhanced HK activity to sustain glucose uptake but reduced activity of FBP1 to block the gluconeogenic route and reduced activity of PFK1 and ENO1 to moderate drop of glucose-6-phosphate and to repartition more carbon flux to pentose phosphate pathway (PPP), maintaining cellular energy and redox homeostasis at cellular and organismal levels.Similar results were also obtained using ULK2 as the kinase (data not shown). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274039 |
Ser88 |
LVMNMLKsSFATCVL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27153534 |
Here, we demonstrate that, during deprivation of amino acid and growth factors, ULK1/2 directly phosphorylate key glycolytic enzymes including hexokinase (HK), phosphofructokinase 1 (PFK1), enolase 1 (ENO1), and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBP1).Phosphorylation of these enzymes leads to enhanced HK activity to sustain glucose uptake but reduced activity of FBP1 to block the gluconeogenic route and reduced activity of PFK1 and ENO1 to moderate drop of glucose-6-phosphate and to repartition more carbon flux to pentose phosphate pathway (PPP), maintaining cellular energy and redox homeostasis at cellular and organismal levels.Similar results were also obtained using ULK2 as the kinase (data not shown). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ULK2 | down-regulates activity
phosphorylation
|
PFKM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274043 |
Ser74 |
EATWESVsMMLQLGG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27153534 |
Here, we demonstrate that, during deprivation of amino acid and growth factors, ULK1/2 directly phosphorylate key glycolytic enzymes including hexokinase (HK), phosphofructokinase 1 (PFK1), enolase 1 (ENO1), and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBP1).Phosphorylation of these enzymes leads to enhanced HK activity to sustain glucose uptake but reduced activity of FBP1 to block the gluconeogenic route and reduced activity of PFK1 and ENO1 to moderate drop of glucose-6-phosphate and to repartition more carbon flux to pentose phosphate pathway (PPP), maintaining cellular energy and redox homeostasis at cellular and organismal levels.Similar results were also obtained using ULK2 as the kinase (data not shown). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274044 |
Ser762 |
YEIDLDTsDHAHLEH |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27153534 |
Here, we demonstrate that, during deprivation of amino acid and growth factors, ULK1/2 directly phosphorylate key glycolytic enzymes including hexokinase (HK), phosphofructokinase 1 (PFK1), enolase 1 (ENO1), and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBP1).Phosphorylation of these enzymes leads to enhanced HK activity to sustain glucose uptake but reduced activity of FBP1 to block the gluconeogenic route and reduced activity of PFK1 and ENO1 to moderate drop of glucose-6-phosphate and to repartition more carbon flux to pentose phosphate pathway (PPP), maintaining cellular energy and redox homeostasis at cellular and organismal levels.Similar results were also obtained using ULK2 as the kinase (data not shown). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ULK2 | down-regulates
phosphorylation
|
PRKAB1 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173092 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21460634 |
Ulk1/2 in turn phosphorylates all three subunits of ampk and thereby negatively regulates its activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK2 | down-regulates
phosphorylation
|
PRKAA2 |
0.309 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173089 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21460634 |
We could prove that ulk1-mediated phosphorylation of ampk reduced its level of phosphorylation at t172 of the _-subunit and hence interferes with its catalytic activity. I |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MTOR | down-regulates
phosphorylation
|
ULK2 |
0.768 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183961 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19211836 |
Mtor phosphorylates a mammalian homologue of atg13 and the mammalian atg1 homologues ulk1 and ulk2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK2 | down-regulates
phosphorylation
|
PRKAG3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173095 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21460634 |
Ulk1/2 in turn phosphorylates all three subunits of ampk and thereby negatively regulates its activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK2 | up-regulates
phosphorylation
|
ATG13 |
0.741 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184126 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19225151 |
Ulks directly phosphorylates atg13. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK2 | down-regulates
phosphorylation
|
AMPK |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217487 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21460634 |
We could prove that ulk1-mediated phosphorylation of ampk reduced its level of phosphorylation at t172 of the _-subunit and hence interferes with its catalytic activity. I |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATG13 | up-regulates
binding
|
ULK2 |
0.741 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184123 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19225151 |
He mammalian atg13 binds both ulk1 and ulk2 and mediates the interaction of the ulk proteins with fip200. The binding of atg13 stabilizes and activates ulk and facilitates the phosphorylation of fip200 by ulk |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ULK2
- 
- 