| + |
MELK | up-regulates 
phosphorylation
|
CDC25B |
0.549 |
| 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 |
0.549 |
| 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 |
0.334 |
| 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 |
0.27 |
| 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 |
3.0
MELK
- 
- 