| + |
MELK | up-regulates 
phosphorylation
|
CDC25B |
0.533 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-137378 |
Ser169 |
VLRNITNsQAPDGRR |
Homo sapiens |
|
| pmid |
sentence |
| 15908796 |
We demonstrate that cdc25b is phosphorylated in vitro by peg3 on serine 169this phosphorylated form of cdc25b accumulates during mitosis, and is localized to the centrosomes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MELK | up-regulates
phosphorylation
|
MELK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140958 |
Ser171 |
HLQTCCGsLAYAAPE |
Homo sapiens |
|
| pmid |
sentence |
| 16216881 |
We have mapped no less than 16 autophosphorylation sites including serines, threonines, and a tyrosine residue and show that the phosphorylation of thr167 and ser171 is required for the activation of melk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140998 |
Ser356 |
DIKSNNWsLEDVTAS |
Homo sapiens |
|
| pmid |
sentence |
| 16216881 |
We have mapped no less than 16 autophosphorylation sites including serines, threonines, and a tyrosine residue and show that the phosphorylation of thr167 and ser171 is required for the activation of melk.We have not yet explored the role of autophosphorylation of nine residues in the c-terminal, autoinhibitory domain (fig. 4c). An enticing hypothesis is that these autophosphorylations decrease the inhibitory potency of this domain and thereby contribute to the activation of the kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141002 |
Ser391 |
GAATPRTsQFTKYWT |
Homo sapiens |
|
| pmid |
sentence |
| 16216881 |
We have mapped no less than 16 autophosphorylation sites including serines, threonines, and a tyrosine residue and show that the phosphorylation of thr167 and ser171 is required for the activation of melk.We have not yet explored the role of autophosphorylation of nine residues in the c-terminal, autoinhibitory domain (fig. 4c). An enticing hypothesis is that these autophosphorylations decrease the inhibitory potency of this domain and thereby contribute to the activation of the kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141006 |
Ser407 |
SNGVESKsLTPALCR |
Homo sapiens |
|
| pmid |
sentence |
| 16216881 |
We have mapped no less than 16 autophosphorylation sites including serines, threonines, and a tyrosine residue and show that the phosphorylation of thr167 and ser171 is required for the activation of melk.We have not yet explored the role of autophosphorylation of nine residues in the c-terminal, autoinhibitory domain (fig. 4c). An enticing hypothesis is that these autophosphorylations decrease the inhibitory potency of this domain and thereby contribute to the activation of the kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141010 |
Ser431 |
ENVYTPKsAVKNEEY |
Homo sapiens |
|
| pmid |
sentence |
| 16216881 |
We have mapped no less than 16 autophosphorylation sites including serines, threonines, and a tyrosine residue and show that the phosphorylation of thr167 and ser171 is required for the activation of melk.We have not yet explored the role of autophosphorylation of nine residues in the c-terminal, autoinhibitory domain (fig. 4c). An enticing hypothesis is that these autophosphorylations decrease the inhibitory potency of this domain and thereby contribute to the activation of the kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141014 |
Ser505 |
SPERRCRsVELDLNQ |
Homo sapiens |
|
| pmid |
sentence |
| 16216881 |
We have mapped no less than 16 autophosphorylation sites including serines, threonines, and a tyrosine residue and show that the phosphorylation of thr167 and ser171 is required for the activation of melk.We have not yet explored the role of autophosphorylation of nine residues in the c-terminal, autoinhibitory domain (fig. 4c). An enticing hypothesis is that these autophosphorylations decrease the inhibitory potency of this domain and thereby contribute to the activation of the kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141018 |
Ser529 |
KGAKVFGsLERGLDK |
Homo sapiens |
|
| pmid |
sentence |
| 16216881 |
We have mapped no less than 16 autophosphorylation sites including serines, threonines, and a tyrosine residue and show that the phosphorylation of thr167 and ser171 is required for the activation of melk.We have not yet explored the role of autophosphorylation of nine residues in the c-terminal, autoinhibitory domain (fig. 4c). An enticing hypothesis is that these autophosphorylations decrease the inhibitory potency of this domain and thereby contribute to the activation of the kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141022 |
Thr167 |
NKDYHLQtCCGSLAY |
Homo sapiens |
|
| pmid |
sentence |
| 16216881 |
We have mapped no less than 16 autophosphorylation sites including serines, threonines, and a tyrosine residue and show that the phosphorylation of thr167 and ser171 is required for the activation of melk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141026 |
Thr398 |
SQFTKYWtESNGVES |
Homo sapiens |
|
| pmid |
sentence |
| 16216881 |
We have mapped no less than 16 autophosphorylation sites including serines, threonines, and a tyrosine residue and show that the phosphorylation of thr167 and ser171 is required for the activation of melk.We have not yet explored the role of autophosphorylation of nine residues in the c-terminal, autoinhibitory domain (fig. 4c). An enticing hypothesis is that these autophosphorylations decrease the inhibitory potency of this domain and thereby contribute to the activation of the kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141030 |
Thr494 |
TGTDKLMtGVISPER |
Homo sapiens |
|
| pmid |
sentence |
| 16216881 |
We have mapped no less than 16 autophosphorylation sites including serines, threonines, and a tyrosine residue and show that the phosphorylation of thr167 and ser171 is required for the activation of melk.We have not yet explored the role of autophosphorylation of nine residues in the c-terminal, autoinhibitory domain (fig. 4c). An enticing hypothesis is that these autophosphorylations decrease the inhibitory potency of this domain and thereby contribute to the activation of the kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141034 |
Thr539 |
RGLDKVItVLTRSKR |
Homo sapiens |
|
| pmid |
sentence |
| 16216881 |
We have mapped no less than 16 autophosphorylation sites including serines, threonines, and a tyrosine residue and show that the phosphorylation of thr167 and ser171 is required for the activation of melk.We have not yet explored the role of autophosphorylation of nine residues in the c-terminal, autoinhibitory domain (fig. 4c). An enticing hypothesis is that these autophosphorylations decrease the inhibitory potency of this domain and thereby contribute to the activation of the kinase. |
|
| Publications: |
11 |
Organism: |
Homo Sapiens |
| + |
MELK | down-regulates activity 
phosphorylation
|
CDC25B |
0.533 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255655 |
Ser219 |
HALAEWAsRREAFAQ |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12400006 |
In the present study we show that the human pEg3 kinase is able to specifically phosphorylate CDC25B in vitro. One phosphorylation site was identified and corresponded to serine 323[Ä] Taken together these results suggest that pEg3 is a potential regulator of the G2/M progression and may act antagonistically to the CDC25B phosphatase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MELK | up-regulates quantity by stabilization
phosphorylation
|
EZH2 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277480 |
Ser220 |
RPPRKFPsDKIFEAI |
Homo sapiens |
Natural Killer Cell Line |
| pmid |
sentence |
| 31434700 |
We observed a MELK-mediated increase of EZH2 S220 phosphorylation along with a concomitant loss of EZH2 K222 ubiquitination, suggesting a phosphorylation-dependent regulation of EZH2 ubiquitination. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
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 |
| + |
MELK | down-regulates activity
phosphorylation
|
PDPK1 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276414 |
Thr354 |
WENLHQQtPPKLTAY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22544756 |
The results showed that MPK38 interacted with and inhibited PDK1 activity via Thr(354) phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MELK | down-regulates quantity
phosphorylation
|
FOXO3 |
0.361 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279375 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28938528 |
Further analysis indicated that FOXO1 and FOXO3, two known transcriptional regulators of p21, were phosphorylated by MELK and thus be involved in the induction of p21 after MELK inhibition.|Our findings revealed that siRNA mediated MELK knockdown increased protein levels of FOXO1 and FOXO3, which might increase p21 transcriptional level in a p53 independent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MELK | down-regulates quantity
phosphorylation
|
FOXO1 |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279543 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28938528 |
Direct phosphorylation of FOXO1 and FOXO3 by MELK.|Our findings revealed that siRNA mediated MELK knockdown increased protein levels of FOXO1 and FOXO3, which might increase p21 transcriptional level in a p53 independent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MELK | up-regulates activity
phosphorylation
|
FOXM1 |
0.5 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278412 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23404835 |
MELK Activates FOXM1 Transcriptional Activity Leading to Upregulation of Mitotic Gene Expression.|The autoradiogram clearly shows in vitro phosphorylation of FOXM1 by MELK and CDK2 and cyclinA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MELK | up-regulates activity
phosphorylation
|
PTK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279230 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24885567 |
As the aforementioned results showed that MELK promotes FAK phosphorylation, and it is well known that FAK is an important regulator of cell migration and invasion, we speculated that MELK could regulate cell migration and invasion via the FAK/Paxillin pathway.|Finally, knockdown of MELK decreased the phosphorylation of the FAK and paxillin, and prevented gastrin stimulated FAK and paxillin phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MELK | up-regulates activity
phosphorylation
|
SQSTM1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279544 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29212029 |
Consistent with our SILAC experiments, MELK directly phosphorylated SQSTM1 (XREF_FIG).|Furthermore, we show that MELK promotes melanoma growth by activating NF-kappaB pathway activity via Sequestosome 1 (SQSTM1 and p62). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
MELK
- 
- 