| + |
STK11 | up-regulates 
phosphorylation
|
TP53 |
0.747 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150830 |
Ser15 |
PSVEPPLsQETFSDL |
Homo sapiens |
|
| pmid |
sentence |
| 17108107 |
We show that lkb1 physically associates with p53 in the nucleus and directly or indirectly phosphorylates p53 ser15 (previously shown to be phosphorylated by amp-dependent kinase) and p53 ser392 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150834 |
Ser392 |
FKTEGPDsD |
Homo sapiens |
|
| pmid |
sentence |
| 17108107 |
We show that lkb1 physically associates with p53 in the nucleus and directly or indirectly phosphorylates p53 ser15 (previously shown to be phosphorylated by amp-dependent kinase) and p53 ser392 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling |
| + |
STK11 | up-regulates activity
phosphorylation
|
MARK3 |
0.32 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104059 |
Ser215 |
KLDTFCGsPPYAAPE |
Homo sapiens |
HeLa-S3 Cell |
| pmid |
sentence |
| 12879020 |
Regulation of the wnt signalling component par1a by the peutz-jeghers syndrome kinase lkb1. Lkb1 is a master kinase that activates 13 kinases of the ampk subfamily, including mark/par-1. Mark3 is activated by phosphorylation on thr-211. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104063 |
Thr211 |
TVGGKLDtFCGSPPY |
Homo sapiens |
HeLa-S3 Cell |
| pmid |
sentence |
| 12879020 |
Regulation of the wnt signalling component par1a by the peutz-jeghers syndrome kinase lkb1. Lkb1 is a master kinase that activates 13 kinases of the ampk subfamily, including mark/par-1. Mark3 is activated by phosphorylation on thr-211. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates
phosphorylation
|
STK11 |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185640 |
Ser307 |
IRQIRQHsWFRKKHP |
Homo sapiens |
|
| pmid |
sentence |
| 19414597 |
Here, we have identified s307 as a novel phosphorylation site in lkb1 and provide evidence that, in multiple cell types, phosphorylation of this site by protein kinase c ? (pkc-?) Induces nucleocytoplasmic transport of lkb1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle, Smooth Muscle |
| + |
STK11 | down-regulates activity 
phosphorylation
|
PTEN |
0.623 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161118 |
Ser380 |
EPDHYRYsDTTDSDP |
Homo sapiens |
|
| pmid |
sentence |
| 21779440 |
The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161122 |
Thr382 |
DHYRYSDtTDSDPEN |
Homo sapiens |
|
| pmid |
sentence |
| 21779440 |
The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161126 |
Thr383 |
HYRYSDTtDSDPENE |
Homo sapiens |
|
| pmid |
sentence |
| 18321849 |
The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
STK11 |
phosphorylation
|
PTEN |
0.623 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247446 |
Ser385 |
RYSDTTDsDPENEPF |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 15987703 |
We provide evidence suggesting that LKB1 phosphorylates PTEN at residue S385 in combination either with S380, T382 or T383 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6K | down-regulates activity
phosphorylation
|
STK11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252805 |
Ser428 |
SSKIRRLsACKQQ |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 25846811 |
Negative regulation of the LKB1/AMPK pathway by ERK in human acute myeloid leukemia cellsBRAFV600E activates downstream molecules, including ERK and p90 ribosomal S6 kinase (RSK), and leads to the phosphorylation of LKB-1 at Ser428 by these kinases. This cascade results in the dissociation of LKB1 from AMPK. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling |
| + |
ERK1/2 | down-regulates activity
phosphorylation
|
STK11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244595 |
Ser428 |
SSKIRRLsACKQQ |
Homo sapiens |
|
| pmid |
sentence |
| 25846811 |
Directly and/or through the activation of p90RSK, ERK phosphorylates LKB-1 at Ser325 and Ser428. The phosphorylation of LKB-1 causes the dissociation of LKB-1 from AMPK, resulting in the impaired activation of AMPK. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | AMPK Signaling, FLT3-ITD signaling |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
STK11 |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160681 |
Ser428 |
SSKIRRLsACKQQ |
Homo sapiens |
|
| pmid |
sentence |
| 18250273 |
We conclude that pkc-zeta phosphorylates lkb1 at ser428, resulting in lkb1 nuclear export and hence ampk activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates activity
phosphorylation
|
STK11 |
0.412 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209876 |
Ser428 |
SSKIRRLsACKQQ |
Homo sapiens |
|
| pmid |
sentence |
| 25846811 |
Directly and/or through the activation of p90RSK, ERK phosphorylates LKB-1 at Ser325 and Ser428. The phosphorylation of LKB-1 causes the dissociation of LKB-1 from AMPK, resulting in the impaired activation of AMPK. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates activity
phosphorylation
|
STK11 |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250055 |
Ser428 |
SSKIRRLsACKQQ |
Rattus norvegicus |
|
| pmid |
sentence |
| 11297520 |
Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein kinase, but not its farnesylation at Cys(433), is essential for LKB1 to suppress cell growth. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
RPS6KA1 | down-regulates activity
phosphorylation
|
STK11 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209871 |
Ser428 |
SSKIRRLsACKQQ |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 25846811 |
Negative regulation of the LKB1/AMPK pathway by ERK in human acute myeloid leukemia cellsBRAFV600E activates downstream molecules, including ERK and p90 ribosomal S6 kinase (RSK), and leads to the phosphorylation of LKB-1 at Ser428 by these kinases. This cascade results in the dissociation of LKB1 from AMPK. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | AMPK Signaling, FLT3-ITD signaling |
| + |
MAPK3 | down-regulates activity
phosphorylation
|
STK11 |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209880 |
Ser428 |
SSKIRRLsACKQQ |
Homo sapiens |
|
| pmid |
sentence |
| 25846811 |
Directly and/or through the activation of p90RSK, ERK phosphorylates LKB-1 at Ser325 and Ser428. The phosphorylation of LKB-1 causes the dissociation of LKB-1 from AMPK, resulting in the impaired activation of AMPK. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates activity
phosphorylation
|
SIRT1 |
0.591 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277322 |
Ser615 |
GEKNERTsVAGTVRK |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34216621 |
Resveratrol promotes the binding between LKB1 and Sirt1, which we first reported, and this binding leads to LKB1-mediated phosphorylation of Sirt1 at three different serine residues in the C terminus of Sirt1. Mechanistically, LKB1-mediated phosphorylation increases intramolecular interactions in Sirt1, such as the binding of the C terminus to the deacetylase core domain, thereby eliminating DBC1 (Deleted in Breast Cancer 1, Sirt1 endogenous inhibitor) inhibition and promoting Sirt1-substrate interaction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277321 |
Ser669 |
EDDVLSSsSCGSNSD |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34216621 |
Resveratrol promotes the binding between LKB1 and Sirt1, which we first reported, and this binding leads to LKB1-mediated phosphorylation of Sirt1 at three different serine residues in the C terminus of Sirt1. Mechanistically, LKB1-mediated phosphorylation increases intramolecular interactions in Sirt1, such as the binding of the C terminus to the deacetylase core domain, thereby eliminating DBC1 (Deleted in Breast Cancer 1, Sirt1 endogenous inhibitor) inhibition and promoting Sirt1-substrate interaction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277323 |
Ser732 |
EAINEAIsVKQEVTD |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34216621 |
Resveratrol promotes the binding between LKB1 and Sirt1, which we first reported, and this binding leads to LKB1-mediated phosphorylation of Sirt1 at three different serine residues in the C terminus of Sirt1. Mechanistically, LKB1-mediated phosphorylation increases intramolecular interactions in Sirt1, such as the binding of the C terminus to the deacetylase core domain, thereby eliminating DBC1 (Deleted in Breast Cancer 1, Sirt1 endogenous inhibitor) inhibition and promoting Sirt1-substrate interaction. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | AMPK Signaling |
| + |
STK11 | down-regulates
phosphorylation
|
PAK1 |
0.249 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164814 |
Thr109 |
QWARLLQtSNITKSE |
Homo sapiens |
|
| pmid |
sentence |
| 20400510 |
Lkb1 suppresses p21-activated kinase-1 (pak1) by phosphorylation of thr109 in the p21-binding domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates activity
phosphorylation
|
PRMT5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277411 |
Thr139 |
TNLARVLtNHIHTGH |
in vitro |
|
| pmid |
sentence |
| 30289978 |
We found that PRMT5 is a bona fade substrate for LKB1. We identified T132, 139 and 144 residues, located in the TIM-Barrel domain of PRMT5, as target sites for LKB1 phosphorylation. The point mutation of PRMT5 T139/144 to A139/144 drastically decreased its methyltransferase activity, due probably to the loss of its interaction with regulatory proteins such as MEP50, pICln and RiOK1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277412 |
Thr144 |
VLTNHIHtGHHSSMF |
in vitro |
|
| pmid |
sentence |
| 30289978 |
We found that PRMT5 is a bona fade substrate for LKB1. We identified T132, 139 and 144 residues, located in the TIM-Barrel domain of PRMT5, as target sites for LKB1 phosphorylation. The point mutation of PRMT5 T139/144 to A139/144 drastically decreased its methyltransferase activity, due probably to the loss of its interaction with regulatory proteins such as MEP50, pICln and RiOK1. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
STK11 | up-regulates
phosphorylation
|
MELK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141038 |
Thr167 |
NKDYHLQtCCGSLAY |
Homo sapiens |
|
| pmid |
sentence |
| 16216881 |
Site-directed mutagenesis indicated that thr167 and ser171, located between the dfg and ape motifs in the activation loop or t-loop, need to be autophosphorylated for melk to be active as a protein kinase (fig. 5). These sites are conserved in all other ampk-related protein kinases (fig. 4a), and the site corresponding to thr167 has been shown to be phosphorylated by protein kinase lkb1 (5). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates
phosphorylation
|
PRKAA2 |
0.611 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119179 |
Thr172 |
SDGEFLRtSCGSPNY |
Homo sapiens |
|
| pmid |
sentence |
| 14614828 |
We demonstrated that lkb1 phosphorylates ampk on the activation loop threonine (thr172) within the catalytic subunit and activates ampk in vitro. Here, we have investigated whether lkb1 corresponds to the major ampkk activity present in cell extracts. Ampkk purified from rat liver corresponds to lkb1, and blocking lkb1 activity in cells abolishes ampk activation in response to different stimuli |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122725 |
Thr172 |
SDGEFLRtSCGSPNY |
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
We demonstrated that lkb1 phosphorylates ampk on the activation loop threonine (thr172) within the catalytic subunit and activates ampk in vitro. Here, we have investigated whether lkb1 corresponds to the major ampkk activity present in cell extracts. Ampkk purified from rat liver corresponds to lkb1, and blocking lkb1 activity in cells abolishes ampk activation in response to different stimuli |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates activity
phosphorylation
|
SNRK |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260824 |
Thr173 |
QPGKKLTtSCGSLAY |
Homo sapiens |
|
| pmid |
sentence |
| 15733851 |
We demonstrate that LKB1 activates SNRK by phosphorylating the T‐loop residue (Thr173) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247493 |
Thr173 |
QPGKKLTtSCGSLAY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15733851 |
we identify the sucrose non-fermenting protein (SNF1)-related kinase (SNRK), a largely unstudied AMPK subfamily member, as a novel substrate for LKB1. We demonstrate that LKB1 activates SNRK by phosphorylating the T-loop residue (Thr173), |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates
phosphorylation
|
BRSK2 |
0.481 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122485 |
Thr174 |
VGDSLLEtSCGSPHY |
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
Lkb1 is a master kinase that activates 13 kinases of the ampk subfamily, including mark/par-1we recently demonstrated that the lkb1 tumour suppressor kinase, in complex with the pseudokinase strad and the scaffolding protein mo25, phosphorylates and activates amp-activated protein kinase (ampk). A total of 12 human kinases (nuak1, nuak2, brsk1, brsk2, qik, qsk, sik, mark1, mark2, mark3, mark4 and melk) are related to ampk. Here we demonstrate that lkb1 can phosphorylate the t-loop of all the members of this subfamily, apart from melk, increasing their activity >50-fold |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates
phosphorylation
|
SIK2 |
0.458 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122788 |
Thr175 |
KSGELLAtWCGSPPY |
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
A total of 12 human kinases (nuak1, nuak2, brsk1, brsk2, qik, qsk, sik, mark1, mark2, mark3, mark4 and melk) are related to ampk. Here we demonstrate that lkb1 can phosphorylate the t-loop of all the members of this subfamily, apart from melk, increasing their activity >50-fold. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates
phosphorylation
|
SIK1 |
0.566 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122784 |
Thr182 |
KSGEPLStWCGSPPY |
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
Lkb1 is a master kinase that activates 13 kinases of the ampk subfamily, including mark/par-1we recently demonstrated that the lkb1 tumour suppressor kinase, in complex with the pseudokinase strad and the scaffolding protein mo25, phosphorylates and activates amp-activated protein kinase (ampk). A total of 12 human kinases (nuak1, nuak2, brsk1, brsk2, qik, qsk, sik, mark1, mark2, mark3, mark4 and melk) are related to ampk. Here we demonstrate that lkb1 can phosphorylate the t-loop of all the members of this subfamily, apart from melk, increasing their activity >50-fold |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates activity
phosphorylation
|
SIK1 |
0.566 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262844 |
Thr182 |
KSGEPLStWCGSPPY |
Homo sapiens |
|
| pmid |
sentence |
| 18946175 |
Salt inducible kinase (SIK) 1, a member of the AMP-activated kinase (AMPK) family, is activated by the AMPK-activator LKB1 which phosphorylates SIK1 at Thr182. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates activity
phosphorylation
|
PRKAA1 |
0.581 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139297 |
Thr183 |
SDGEFLRtSCGSPNY |
in vitro |
|
| pmid |
sentence |
| 16054095 |
The AMP-activated protein kinase (AMPK) is a critical regulator of energy balance at both the cellular and whole-body levels. Two upstream kinases have been reported to activate AMPK in cell-free assays, i.e., the tumor suppressor LKB1 and calmodulin-dependent protein kinase kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122721 |
Thr183 |
SDGEFLRtSCGSPNY |
in vitro |
|
| pmid |
sentence |
| 14976552 |
We recently demonstrated that the LKB1 tumour suppressor kinase, in complex with the pseudokinase STRAD and the scaffolding protein MO25, phosphorylates and activates AMP_activated protein kinase (AMPK). |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
STK11 | up-regulates activity
phosphorylation
|
STK11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101840 |
Thr185 |
KPGNLLLtTGGTLKI |
Homo sapiens |
HEK-293 Cell, HeLa Cell |
| pmid |
sentence |
| 12805220 |
It was shown that thr336 and thr366 are the major autophosphorylation sites of mouse lkb1 (sapkota et al., 2002). We confirmed these data on the human orthologues thr336 and thr363. Moreover, the enhanced stoichiometry of lkb1 autophosphorylation by strad enabled us to identify two novel sites: thr185 and thr402. We show that increased lkb1 autophosphorylation of all sites correlates with the activation of its catalytic activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101844 |
Thr336 |
KDRWRSMtVVPYLED |
Homo sapiens |
HEK-293 Cell, HeLa Cell |
| pmid |
sentence |
| 12805220 |
It was shown that thr336 and thr366 are the major autophosphorylation sites of mouse lkb1 (sapkota et al., 2002). We confirmed these data on the human orthologues thr336 and thr363. Moreover, the enhanced stoichiometry of lkb1 autophosphorylation by strad enabled us to identify two novel sites: thr185 and thr402. We show that increased lkb1 autophosphorylation of all sites correlates with the activation of its catalytic activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101848 |
Thr363 |
IEDDIIYtQDFTVPG |
Homo sapiens |
HEK-293 Cell, HeLa Cell |
| pmid |
sentence |
| 12805220 |
It was shown that thr336 and thr366 are the major autophosphorylation sites of mouse lkb1 (sapkota et al., 2002). We confirmed these data on the human orthologues thr336 and thr363. Moreover, the enhanced stoichiometry of lkb1 autophosphorylation by strad enabled us to identify two novel sites: thr185 and thr402. We show that increased lkb1 autophosphorylation of all sites correlates with the activation of its catalytic activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101852 |
Thr402 |
TEAAQLStKSRAEGR |
Homo sapiens |
HEK-293 Cell, HeLa Cell |
| pmid |
sentence |
| 12805220 |
It was shown that thr336 and thr366 are the major autophosphorylation sites of mouse lkb1 (sapkota et al., 2002). We confirmed these data on the human orthologues thr336 and thr363. Moreover, the enhanced stoichiometry of lkb1 autophosphorylation by strad enabled us to identify two novel sites: thr185 and thr402. We show that increased lkb1 autophosphorylation of all sites correlates with the activation of its catalytic activity. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | AMPK Signaling, FLT3-ITD signaling |
| + |
STK11 | down-regulates activity
phosphorylation
|
STK11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109028 |
Thr189 |
LLLTTGGtLKISDLG |
Homo sapiens |
|
| pmid |
sentence |
| 11430832 |
These data suggest that the phosphorylation of thr-189 negatively regulates lkb1 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Intestinal Epithelium |
| Pathways: | AMPK Signaling, FLT3-ITD signaling |
| + |
STK11 | up-regulates
phosphorylation
|
BRSK1 |
0.463 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122413 |
Thr189 |
VGDSLLEtSCGSPHY |
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
Lkb1 is a master kinase that activates 13 kinases of the ampk subfamily, including mark/par-1we recently demonstrated that the lkb1 tumour suppressor kinase, in complex with the pseudokinase strad and the scaffolding protein mo25, phosphorylates and activates amp-activated protein kinase (ampk). A total of 12 human kinases (nuak1, nuak2, brsk1, brsk2, qik, qsk, sik, mark1, mark2, mark3, mark4 and melk) are related to ampk. Here we demonstrate that lkb1 can phosphorylate the t-loop of all the members of this subfamily, apart from melk, increasing their activity >50-fold |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates activity
phosphorylation
|
MARK2 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276165 |
Thr208 |
TFGNKLDtFCGSPPY |
in vitro |
|
| pmid |
sentence |
| 18424437 |
MARK family kinases can be activated by phosphorylation of a conserved threonine (Thr-208 in MARK2), and inactivated by phosphorylation of a serine (Ser-212), both in the activation loop of the catalytic domain. Activation is achieved by the kinases MARKK/TAO1 or LKB1, although the inactivating kinase was unknown. We show here that GSK3beta serves the role of the inhibitory kinase. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STK11 | up-regulates
phosphorylation
|
MARK2 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122628 |
Thr208 |
TFGNKLDtFCGSPPY |
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
Lkb1 is a master kinase that activates 13 kinases of the ampk subfamily, including mark/par-1we recently demonstrated that the lkb1 tumour suppressor kinase, in complex with the pseudokinase strad and the scaffolding protein mo25, phosphorylates and activates amp-activated protein kinase (ampk). A total of 12 human kinases (nuak1, nuak2, brsk1, brsk2, qik, qsk, sik, mark1, mark2, mark3, mark4 and melk) are related to ampk. Here we demonstrate that lkb1 can phosphorylate the t-loop of all the members of this subfamily, apart from melk, increasing their activity >50-fold |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156126 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17573348 |
Here we show in vitro that lkb1 phosphorylates and activates mark2 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates
phosphorylation
|
NUAK2 |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122717 |
Thr208 |
HQGKFLQtFCGSPLY |
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
A total of 12 human kinases (nuak1, nuak2, brsk1, brsk2, qik, qsk, sik, mark1, mark2, mark3, mark4 and melk) are related to ampk. Here we demonstrate that lkb1 can phosphorylate the t-loop of all the members of this subfamily, apart from melk, increasing their activity >50-fold. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates
phosphorylation
|
NUAK1 |
0.526 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122686 |
Thr211 |
QKDKFLQtFCGSPLY |
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
A total of 12 human kinases (nuak1, nuak2, brsk1, brsk2, qik, qsk, sik, mark1, mark2, mark3, mark4 and melk) are related to ampk. Here we demonstrate that lkb1 can phosphorylate the t-loop of all the members of this subfamily, apart from melk, increasing their activity >50-fold. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates
phosphorylation
|
MARK4 |
0.515 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122682 |
Thr214 |
TLGSKLDtFCGSPPY |
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
Lkb1 is a master kinase that activates 13 kinases of the ampk subfamily, including mark/par-1we recently demonstrated that the lkb1 tumour suppressor kinase, in complex with the pseudokinase strad and the scaffolding protein mo25, phosphorylates and activates amp-activated protein kinase (ampk). A total of 12 human kinases (nuak1, nuak2, brsk1, brsk2, qik, qsk, sik, mark1, mark2, mark3, mark4 and melk) are related to ampk. Here we demonstrate that lkb1 can phosphorylate the t-loop of all the members of this subfamily, apart from melk, increasing their activity >50-fold |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates
phosphorylation
|
MARK1 |
0.42 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122545 |
Thr215 |
TVGNKLDtFCGSPPY |
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
Lkb1 is a master kinase that activates 13 kinases of the ampk subfamily, including mark/par-1we recently demonstrated that the lkb1 tumour suppressor kinase, in complex with the pseudokinase strad and the scaffolding protein mo25, phosphorylates and activates amp-activated protein kinase (ampk). A total of 12 human kinases (nuak1, nuak2, brsk1, brsk2, qik, qsk, sik, mark1, mark2, mark3, mark4 and melk) are related to ampk. Here we demonstrate that lkb1 can phosphorylate the t-loop of all the members of this subfamily, apart from melk, increasing their activity >50-fold |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates
phosphorylation
|
SIK3 |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122835 |
Thr221 |
TPGQLLKtWCGSPPY |
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
Lkb1 is a master kinase that activates 13 kinases of the ampk subfamily, including mark/par-1we recently demonstrated that the lkb1 tumour suppressor kinase, in complex with the pseudokinase strad and the scaffolding protein mo25, phosphorylates and activates amp-activated protein kinase (ampk). A total of 12 human kinases (nuak1, nuak2, brsk1, brsk2, qik, qsk, sik, mark1, mark2, mark3, mark4 and melk) are related to ampk. Here we demonstrate that lkb1 can phosphorylate the t-loop of all the members of this subfamily, apart from melk, increasing their activity >50-fold |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates activity
phosphorylation
|
STRADA |
0.938 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261950 |
Thr329 |
GLSDSLTtSTPRPSN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12805220 |
Endogenous LKB1 and STRAD form a complex in which STRAD activates LKB1, resulting in phosphorylation of both partners.LKB1 phosphorylates STRAD at Thr329 and Thr419 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247564 |
Thr419 |
SGIFGLVtNLEELEV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12805220 |
Endogenous LKB1 and STRAD form a complex in which STRAD activates LKB1, resulting in phosphorylation of both partners.LKB1 phosphorylates STRAD at Thr329 and Thr419 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | AMPK Signaling |
| + |
ATM |
phosphorylation
|
STK11 |
0.589 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-92877 |
Thr363 |
IEDDIIYtQDFTVPG |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 12234250 |
We demonstrate that both dna-pk and atm efficiently phosphorylate lkb1 at thr-366 in vitro and provide evidence that atm mediates this phosphorylation in vivo. however, phosphorylation of lkb1 at thr-366 may have some role in enabling lkb1 to suppress cell growth |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling |
| + |
ATM | up-regulates
phosphorylation
|
STK11 |
0.589 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-92873 |
Thr367 |
IIYTQDFtVPGQVPE |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 12234250 |
We demonstrate that both dna-pk and atm efficiently phosphorylate lkb1 at thr-366 in vitro and provide evidence that atm mediates this phosphorylation in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling |
| + |
FOXO3 | down-regulates quantity
transcriptional regulation
|
STK11 |
0.623 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255758 |
|
|
|
|
| pmid |
sentence |
| 22848740 |
SGK-1 Negatively Regulates LKB1 Expression via FOXO3 Transcription Factor |
|
| Publications: |
1 |
| Pathways: | AMPK Signaling |
| + |
STRADA | up-regulates activity
binding
|
STK11 |
0.938 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247560 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12805220 |
Endogenous LKB1 and STRAD form a complex in which STRAD activates LKB1, resulting in phosphorylation of both partners.LKB1 phosphorylates STRAD at Thr329 and Thr419 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | AMPK Signaling |
| + |
STK11 | down-regulates quantity 
transcriptional regulation
|
CPS1 |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267919 |
|
|
Homo sapiens |
Non-small Cell Lung Cancer Cell Line |
| pmid |
sentence |
| 28538732 |
LKB1 negatively regulates CPS1 transcription |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates
phosphorylation
|
AMPK |
0.595 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217469 |
|
|
in vitro |
|
| pmid |
sentence |
| 14614828 |
We demonstrated that lkb1 phosphorylates ampk on the activation loop threonine (thr172) within the catalytic subunit and activates ampk in vitro. Here, we have investigated whether lkb1 corresponds to the major ampkk activity present in cell extracts. Ampkk purified from rat liver corresponds to lkb1, and blocking lkb1 activity in cells abolishes ampk activation in response to different stimuli |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217472 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
We demonstrated that lkb1 phosphorylates ampk on the activation loop threonine (thr172) within the catalytic subunit and activates ampk in vitro. Here, we have investigated whether lkb1 corresponds to the major ampkk activity present in cell extracts. Ampkk purified from rat liver corresponds to lkb1, and blocking lkb1 activity in cells abolishes ampk activation in response to different stimuli |
|
| Publications: |
2 |
Organism: |
In Vitro, Homo Sapiens |
| Pathways: | AMPK Signaling, FLT3-ITD signaling |
| + |
APPL1 | up-regulates
binding
|
STK11 |
0.322 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186065 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19520843 |
In this study, we identified lkb1 as a new binding partner of appl1 and showed that the bar domain of appl1 is involved in this interaction.Here we show that in muscle cells adiponectin and metformin induce ampk activation by promoting appl1-dependent lkb1 cytosolic translocation. Appl1 mediates adiponectin signaling by directly interacting with adiponectin receptors and enhances lkb1 cytosolic localization by anchoring this kinase in the cytosol. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
STK11 | down-regulates
|
GSK3B |
0.386 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119892 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14657655 |
Phospho-gsk3b-specific antibodies also revolved that lkb1 regulates gsk3b phosphorylation at a known inhibitory site, serine-9. This localized phosphorylation is cdc42 and pkc-zeta-dependent. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling |
| + |
Gbeta | down-regulates activity
phosphorylation
|
STK11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270071 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25846811 |
Directly and/or through the activation of p90RSK, ERK phosphorylates LKB-1 at Ser325 and Ser428. The phosphorylation of LKB-1 causes the dissociation of LKB-1 from AMPK, resulting in the impaired activation of AMPK. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates activity
phosphorylation
|
AMPK |
0.595 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242602 |
|
|
in vitro |
|
| pmid |
sentence |
| 14976552 |
We recently demonstrated that the LKB1 tumour suppressor kinase, in complex with the pseudokinase STRAD and the scaffolding protein MO25, phosphorylates and activates AMP_activated protein kinase (AMPK). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | AMPK Signaling, FLT3-ITD signaling |
3.0
STK11
- 
- 