| + |
TRIM27 | down-regulates quantity by destabilization 
ubiquitination
|
ULK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272540 |
Lys569 |
DLHVVRPkLPKPPTD |
Mus musculus |
|
| pmid |
sentence |
| 35670107 |
TRIM27 directly polyubiquitinates ULK1 at K568 and K571 sites with K48-linked ubiquitin chains, with proteasomal turnover maintaining control over basal ULK1 levels |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272541 |
Lys572 |
VVRPKLPkPPTDPLG |
Mus musculus |
|
| pmid |
sentence |
| 35670107 |
TRIM27 directly polyubiquitinates ULK1 at K568 and K571 sites with K48-linked ubiquitin chains, with proteasomal turnover maintaining control over basal ULK1 levels |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
ULK1 | down-regulates activity
phosphorylation
|
ENO1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274030 |
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-274029 |
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 |
| + |
ULK1 | up-regulates activity 
phosphorylation
|
HK1 |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274034 |
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-274033 |
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 |
| + |
ULK1 | up-regulates activity
phosphorylation
|
ATG9A |
0.6 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266369 |
Ser14 |
EYQRLEAsYSDSPPG |
Homo sapiens |
|
| pmid |
sentence |
| 27934868 |
Src phosphorylates mATG9 at Tyr8 to maintain its endocytic and constitutive trafficking in unstressed conditions. In response to starvation, phosphorylation of mATG9 at Tyr8 by Src and at Ser14 by ULK1 functionally cooperate to promote interactions between mATG9 and the AP1/2 complex, leading to redistribution of mATG9 from the plasma membrane and juxta-nuclear region to the peripheral pool for autophagy initiation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266366 |
Ser761 |
QSIPRSAsYPCAAPR |
Homo sapiens |
|
| pmid |
sentence |
| 25266655 |
Our data suggest that the localization of mammalian Atg9A to autophagosomes requires phosphorylation on the C terminus of Atg9A at S761, which creates a 14-3-3ζ docking site. Under basal conditions, this phosphorylation is maintained at a low level and is dependent on both ULK1 and AMPK. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ULK1 | up-regulates activity
phosphorylation
|
FUNDC1 |
0.578 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273606 |
Ser17 |
DYESDDDsYEVLDLT |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 24671035 |
Here, we show that ULK1 is upregulated and translocates to fragmented mitochondria upon mitophagy induction by either hypoxia or mitochondrial uncouplers. At mitochondria, ULK1 interacts with FUNDC1, phosphorylating it at serine 17, which enhances FUNDC1 binding to LC3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK1 | up-regulates quantity by stabilization
phosphorylation
|
SEC23B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265285 |
Ser186 |
SCEGISKsYVFRGTK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 30596474 |
Here, we show that the F-box protein FBXW5 targets SEC23B, a component of COPII, for proteasomal degradation and that this event limits the autophagic flux in the presence of nutrients. In response to starvation, ULK1 phosphorylates SEC23B on Serine 186, preventing the interaction of SEC23B with FBXW5 and, therefore, inhibiting SEC23B degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK1 | up-regulates quantity by stabilization
phosphorylation
|
YAP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277570 |
Ser227 |
VQQNMMNsASGPLPD |
Homo sapiens |
SW-1990 Cell |
| pmid |
sentence |
| 34345207 |
Mechanistically, hypoxia stimulates ULK1 to translocate into nucleus, where it interacts with and phosphorylates yes-associated protein (YAP) at Ser227, resulting in YAP stabilization through blockade of ubiquitin-proteasome system (UPS), which in turn facilitates PKM2 transcription, glycolysis, cell proliferation in vitro as well as PDAC growth in mice. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | up-regulates
phosphorylation
|
ULK1 |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170859 |
Ser317 |
SHLASPPsLGEMQQL |
Homo sapiens |
|
| pmid |
sentence |
| 21205641 |
In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186633 |
Ser317 |
SHLASPPsLGEMQQL |
Homo sapiens |
|
| pmid |
sentence |
| 19584320 |
In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170863 |
Ser556 |
GLGCRLHsAPNLSDL |
Homo sapiens |
|
| pmid |
sentence |
| 21205641 |
In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186637 |
Ser556 |
GLGCRLHsAPNLSDL |
Homo sapiens |
|
| pmid |
sentence |
| 19584320 |
In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170867 |
Ser638 |
FDFPKTPsSQNLLAL |
Homo sapiens |
|
| pmid |
sentence |
| 21205641 |
In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186641 |
Ser638 |
FDFPKTPsSQNLLAL |
Homo sapiens |
|
| pmid |
sentence |
| 19584320 |
In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
AMPK | up-regulates
phosphorylation
|
ULK1 |
0.469 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216453 |
Ser317 |
SHLASPPsLGEMQQL |
Homo sapiens |
|
| pmid |
sentence |
| 21205641 |
In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216491 |
Ser317 |
SHLASPPsLGEMQQL |
Homo sapiens |
|
| pmid |
sentence |
| 19584320 |
In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216495 |
Ser556 |
GLGCRLHsAPNLSDL |
Homo sapiens |
|
| pmid |
sentence |
| 19584320 |
In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216457 |
Ser556 |
GLGCRLHsAPNLSDL |
Homo sapiens |
|
| pmid |
sentence |
| 21205641 |
In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216461 |
Ser638 |
FDFPKTPsSQNLLAL |
Homo sapiens |
|
| pmid |
sentence |
| 21205641 |
In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216499 |
Ser638 |
FDFPKTPsSQNLLAL |
Homo sapiens |
|
| pmid |
sentence |
| 19584320 |
In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216464 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21460634 |
Ampk and ulk1 interact and that the latter is phosphorylated by ampk. This phosphorylation leads to the direct activation of ulk1 by ampk bypassing mtor-inhibition. |
|
| Publications: |
7 |
Organism: |
Homo Sapiens |
| Pathways: | MTOR Signaling |
| + |
PBK | down-regulates activity
phosphorylation
|
ULK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277474 |
Ser469 |
IRRSGSTsPLGFARA |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31378785 |
We found that TOPK could directly bind with and phosphorylate ULK1 at Ser469, Ser495, and Ser533. The phosphorylation of ULK1 at Ser469, Ser495, and Ser533 by TOPK decreased the activity and stability of ULK1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277473 |
Ser495 |
GVLARKMsLGGGRPY |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31378785 |
We found that TOPK could directly bind with and phosphorylate ULK1 at Ser469, Ser495, and Ser533. The phosphorylation of ULK1 at Ser469, Ser495, and Ser533 by TOPK decreased the activity and stability of ULK1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277472 |
Ser533 |
AEMRGGRsPRPGSSA |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31378785 |
We found that TOPK could directly bind with and phosphorylate ULK1 at Ser469, Ser495, and Ser533. The phosphorylation of ULK1 at Ser469, Ser495, and Ser533 by TOPK decreased the activity and stability of ULK1. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
ULK1 | up-regulates activity
phosphorylation
|
DENND3 |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264730 |
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-264731 |
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 |
| + |
STK38L | down-regulates quantity
phosphorylation
|
ULK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270348 |
Ser495 |
GVLARKMsLGGGRPY |
Mus musculus |
|
| pmid |
sentence |
| 35670107 |
STK38L ubiquitination promotes its activation and phosphorylation of ULK1 at Ser495, rendering ULK1 in a permissive state for TRIM27-mediated hyper-ubiquitination |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ULK1 | down-regulates activity
phosphorylation
|
FBP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274032 |
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-274031 |
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 |
| + |
ULK1 | down-regulates activity
phosphorylation
|
PFKM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274035 |
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-274036 |
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 |
| + |
MTOR | down-regulates activity
phosphorylation
|
ULK1 |
0.844 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172541 |
Ser758 |
PVVFTVGsPPSGSTP |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 21383122 |
When cells are replenished with rich medium, mtor is activated;it phosphorylates serine 638 and serine 758. The phosphorylation of ulk1 at serine 758 then leads to reassociation between ulk1 and ampk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183903 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21460634 |
mTORC1, which is often referred to as the gatekeeper to autophagy, is a key regulator of the Ulk1-Atg13-FIP200 kinase complex.11,14,25 Under nutrient-rich conditions, active mTORC1 associates with and inactivates the Ulk1-Atg13-FIP200 complex by phosphorylating Ulk1 and Atg13. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187611 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19690328 |
The complementary inhibitory mechanism in which mtorc1 phosphorylates the autophagy regulatory complex containing unc-51-like kinase 1 (ulk1), the mammalian atg13 protein, and focal adhesion kinase interacting protein of 200 kd (fip200) has also been elucidated. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | MTOR Signaling |
| + |
Cullin 3-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
ULK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272417 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26687681 |
Cul3-KLHL20 Ubiquitin Ligase Governs the Turnover of ULK1 and VPS34 Complexes to Control Autophagy Termination. KLHL20 promotes ubiquitination of phagophore-residing VPS34 and Beclin-1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK1 | form complex 
binding
|
ULK1/Atg13/Fip200 |
0.913 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209890 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23863160 |
In mammals, two protein complexes, namely the ULK1-Atg13-FIP200 (200kDa focal adhesion kinase family-interacting protein) complex and the BeclinVps34 complex, function jointly to produce the phagophore membrane, the initial phase of autophagosome formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK1 | down-regulates
phosphorylation
|
AMPK |
0.469 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217484 |
|
|
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 |
| Pathways: | MTOR Signaling |
| + |
ULK1 | down-regulates
phosphorylation
|
PRKAG3 |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173053 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21460634 |
Ulk1/2 in turn phosphorylates all three subunits of ampk and thereby negatively regulates its activity phosphorylation of ampk by ulk1 represents a negative feedback circuit. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMCR8 | down-regulates activity
binding
|
ULK1 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252029 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28195531 |
While focusing on the role of SMCR8 during autophagy initiation, we found that kinase activity and gene expression of ULK1 are increased upon SMCR8 depletion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK1 | up-regulates
phosphorylation
|
ATG13 |
0.915 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183957 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19211835 |
Ulks directly phosphorylate atg13 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRIM27 | down-regulates quantity
ubiquitination
|
ULK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270349 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 35670107 |
STK38L ubiquitination promotes its activation and phosphorylation of ULK1 at Ser495, rendering ULK1 in a permissive state for TRIM27-mediated hyper-ubiquitination |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ULK1 | down-regulates activity
phosphorylation
|
PRKAA1 |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173047 |
|
|
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 |
| + |
ULK1 | up-regulates
phosphorylation
|
AMBRA1 |
0.683 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168292 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20921139 |
When autophagy is induced, ulk1 phosphorylates ambra1, releasing the autophagy core complex from dynein. Its subsequent relocalization to the endoplasmic reticulum enables autophagosome nucleation. Ambra1-dlc1 dissociates from the dynein complex upon ulk1-dependent ambra1 phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK1 | up-regulates
binding
|
GABARAP |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85614 |
|
|
Homo sapiens |
HeLa Cell, Neuron |
| pmid |
sentence |
| 11146101 |
N-terminal proline/serine rich (ps) domain of ulk1 (amino acid 287-416) is required for ulk1-gate-16 and ulk1-gabarap protein interactions |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
ULK1 | down-regulates
phosphorylation
|
PRKAA2 |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173050 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21460634 |
Here we report that ulk1/2 in turn phosphorylates all three subunits of ampk and thereby negatively regulates its activity. Thus, we propose that ulk1 is not only involved in the induction of autophagy, but also in terminating signaling events that trigger autophagy. In our model, phosphorylation of ampk by ulk1 represents a negative feedback circuit. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRAF6 | up-regulates quantity by stabilization
ubiquitination
|
ULK1 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273000 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23524951 |
AMBRA1, interacting with the E3-ligase TRAF6, supports ULK1 ubiquitylation by LYS-63-linked chains, and its subsequent stabilization, self-association and function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK1 | up-regulates
phosphorylation
|
RB1CC1 |
0.911 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186992 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19597335 |
Ulk1 and ulk2 are the kinase phosphorylating their binding proteins atg13 and fip200. Atg13 directly binds fip200 and mediates the interaction between fip200 and ulks. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA1 | up-regulates activity
phosphorylation
|
ULK1 |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173038 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21460634 |
Ampk and ulk1 interact and that the latter is phosphorylated by ampk. This phosphorylation leads to the direct activation of ulk1 by ampk bypassing mtor-inhibition. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAB1A | up-regulates activity
relocalization
|
ULK1 |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261299 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27334615 |
C9orf72 acts as an effector of Rab1a that recruits active Rab1a to theULK1 complex to promote translocation of the ULK1 complex to thephagophore during autophagy initiation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAB1 | up-regulates
phosphorylation
|
ULK1 |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173044 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21460634 |
Ampk and ulk1 interact and that the latter is phosphorylated by ampk. This phosphorylation leads to the direct activation of ulk1 by ampk bypassing mtor-inhibition |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KLHL20 | down-regulates quantity by destabilization
binding
|
ULK1 |
0.252 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272413 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26687681 |
Cul3-KLHL20 Ubiquitin Ligase Governs the Turnover of ULK1 and VPS34 Complexes to Control Autophagy Termination. KLHL20 promotes ubiquitination of phagophore-residing VPS34 and Beclin-1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mTORC1 | down-regulates
phosphorylation
|
ULK1 |
0.624 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217133 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19690328 |
The complementary inhibitory mechanism in which mtorc1 phosphorylates the autophagy regulatory complex containing unc-51-like kinase 1 (ulk1), the mammalian atg13 protein, and focal adhesion kinase interacting protein of 200 kd (fip200) has also been elucidated. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMCR8 | down-regulates quantity
transcriptional regulation
|
ULK1 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252030 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28195531 |
While focusing on the role of SMCR8 during autophagy initiation, we found that kinase activity and gene expression of ULK1 are increased upon SMCR8 depletion. The latter phenotype involved association of SMCR8 with the ULK1 gene locus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ULK1
- 
- 