| + |
PPP1CA | down-regulates activity 
dephosphorylation
|
MECOM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273429 |
Ser1037 |
IGNSNHGsQSPRNVE |
|
|
| pmid |
sentence |
| 23858473 |
We also identified EVI1 phosphorylation sites by MS analysis and showed that Ser538 and Ser858 can be phosphorylated and dephosphorylated by two EVI1 interactome proteins, casein kinase II and protein phosphatase-1α. Finally, mutations that impair EVI1 phosphorylation at these sites reduced EVI1 DNA binding through its C-terminal zinc finger domain and induced cancer cell proliferation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273430 |
Ser726 |
PLKMEPQsPGEVKKL |
|
|
| pmid |
sentence |
| 23858473 |
We also identified EVI1 phosphorylation sites by MS analysis and showed that Ser538 and Ser858 can be phosphorylated and dephosphorylated by two EVI1 interactome proteins, casein kinase II and protein phosphatase-1α. Finally, mutations that impair EVI1 phosphorylation at these sites reduced EVI1 DNA binding through its C-terminal zinc finger domain and induced cancer cell proliferation. |
|
| Publications: |
2 |
| + |
CSNK2A1 | up-regulates activity 
phosphorylation
|
MECOM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273427 |
Ser1037 |
IGNSNHGsQSPRNVE |
|
|
| pmid |
sentence |
| 23858473 |
We also identified EVI1 phosphorylation sites by MS analysis and showed that Ser538 and Ser858 can be phosphorylated and dephosphorylated by two EVI1 interactome proteins, casein kinase II and protein phosphatase-1α. Finally, mutations that impair EVI1 phosphorylation at these sites reduced EVI1 DNA binding through its C-terminal zinc finger domain and induced cancer cell proliferation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273428 |
Ser726 |
PLKMEPQsPGEVKKL |
|
|
| pmid |
sentence |
| 23858473 |
We also identified EVI1 phosphorylation sites by MS analysis and showed that Ser538 and Ser858 can be phosphorylated and dephosphorylated by two EVI1 interactome proteins, casein kinase II and protein phosphatase-1α. Finally, mutations that impair EVI1 phosphorylation at these sites reduced EVI1 DNA binding through its C-terminal zinc finger domain and induced cancer cell proliferation. |
|
| Publications: |
2 |
| + |
ATM | up-regulates activity
phosphorylation
|
MECOM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273433 |
Ser1037 |
IGNSNHGsQSPRNVE |
|
|
| pmid |
sentence |
| 29939287 |
To investigate to what extent EVI1 function might be regulated by post-translational modifications we carried out mass spectrometry- and antibody-based analyses and uncovered an ATM-mediated double phosphorylation of EVI1 at the carboxy-terminal S858/S860 SQS motif. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273434 |
Ser1039 |
NSNHGSQsPRNVEER |
|
|
| pmid |
sentence |
| 29939287 |
To investigate to what extent EVI1 function might be regulated by post-translational modifications we carried out mass spectrometry- and antibody-based analyses and uncovered an ATM-mediated double phosphorylation of EVI1 at the carboxy-terminal S858/S860 SQS motif. |
|
| Publications: |
2 |
| + |
CDK3 | up-regulates activity
phosphorylation
|
MECOM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273431 |
Ser624 |
KMFKDKVsPLQNLAS |
|
|
| pmid |
sentence |
| 33082307 |
The motif harbouring S436 is a target of CDK2 and CDK3 kinases, which interacted with EVI1-WT. The methyltransferase DNMT3A bound preferentially to EVI1-WT compared with EVI1-S436A, and a hypomethylated cell population associated by EVI1-WT expression in murine haematopoietic progenitors is not maintained with EVI1-S436A. |
|
| Publications: |
1 |
| + |
CDK2 | up-regulates activity
phosphorylation
|
MECOM |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273426 |
Ser624 |
KMFKDKVsPLQNLAS |
|
|
| pmid |
sentence |
| 33082307 |
The motif harbouring S436 is a target of CDK2 and CDK3 kinases, which interacted with EVI1-WT. The methyltransferase DNMT3A bound preferentially to EVI1-WT compared with EVI1-S436A, and a hypomethylated cell population associated by EVI1-WT expression in murine haematopoietic progenitors is not maintained with EVI1-S436A. |
|
| Publications: |
1 |
| + |
MLL-AF9 | up-regulates quantity by expression
methylation
|
MECOM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255858 |
|
|
Mus musculus |
Leukemia Cell |
| pmid |
sentence |
| 22553314 |
We hypothesize, based on our ChIP data, that MLL-AF9 up-regulates EVI1 transcription via H3K79 methylation, which is known to be a major gene regulatory mechanism used by some MLL-fusion proteins in leukemia. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML |
| + |
MECOM | up-regulates activity
binding
|
DNMT3A |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273432 |
|
|
|
|
| pmid |
sentence |
| 21695170 |
The oncoprotein EVI1 and the DNA methyltransferase Dnmt3 co-operate in binding and de novo methylation of target DNA|Here we show that EVI1 physically interacts with DNA methyltransferases 3a and 3b (Dnmt3a/b), which are the only de novo DNA methyltransferases identified to date in mouse and man, and that it forms an enzymatically active protein complex that induces de novo DNA methylation in vitro. |
|
| Publications: |
1 |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML |
| + |
MECOM | up-regulates quantity by expression 
transcriptional regulation
|
PBX1 |
0.436 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188155 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 19767769 |
In this study, we identified pbx1, a proto-oncogene in hematopoietic malignancy, as a target gene of evi-1. Overexpression of evi-1 increased pbx1 expression in hematopoietic stem/progenitor cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MECOM | up-regulates quantity by expression
transcriptional regulation
|
ANGPT1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266059 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 15889140 |
We finally observed that the forced expression of Evi1 induced GATA-2 expression in a hematopoietic cell line, EML C1, along with GATA-1, Ang-1, Ang-2 and Tie2 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MECOM | down-regulates
binding
|
SMAD3 |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59132 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9665135 |
Evi-1 interacts with smad3, an intracellular mediator of tgf-beta signalling, thereby suppressing the transcriptional activity of smad3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ub:E2 | up-regulates activity
ubiquitination
|
MECOM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271024 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MECOM | up-regulates quantity by expression
transcriptional regulation
|
TEK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266063 |
|
|
Mus musculus |
Embryonic Cell Line |
| pmid |
sentence |
| 15889140 |
We finally observed that the forced expression of Evi1 induced GATA-2 expression in a hematopoietic cell line, EML C1, along with GATA-1, Ang-1, Ang-2 and Tie2 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RUNX1 | up-regulates quantity by expression
transcriptional regulation
|
MECOM |
0.509 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255715 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22689058 |
Our results suggest that RUNX1 and EVI1 could be regulating each other. RUNX1 would activate EVI1 transcription, and when highly expressed, EVI1 could bind to RUNX1 at protein level, inhibiting its activity as a transcription factor, acting in a negative feedback. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML, MLL fusion protein in AML |
| + |
MECOM | down-regulates activity
binding
|
RUNX1 |
0.509 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255716 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 17575132 |
The results that we present here support this model and show that EVI1 interacts with and inhibits RUNX1. As for GATA1, EVI1 seems to repress RUNX1 function by interacting specifically with its DNA-binding domain Runt, leading to destabilization and dissolution of the DNA-RUNX1 complex. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML, MLL fusion protein in AML |
| + |
MECOM | up-regulates quantity by expression
transcriptional regulation
|
ANGPT2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266060 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 15889140 |
We finally observed that the forced expression of Evi1 induced GATA-2 expression in a hematopoietic cell line, EML C1, along with GATA-1, Ang-1, Ang-2 and Tie2 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MECOM | up-regulates quantity by expression
transcriptional regulation
|
GATA1 |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266061 |
|
|
Mus musculus |
Embryonic Cell Line |
| pmid |
sentence |
| 15889140 |
We finally observed that the forced expression of Evi1 induced GATA-2 expression in a hematopoietic cell line, EML C1, along with GATA-1, Ang-1, Ang-2 and Tie2 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MLL Fusion | up-regulates quantity by expression
methylation
|
MECOM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260107 |
|
|
Mus musculus |
Leukemia Cell |
| pmid |
sentence |
| 22553314 |
We hypothesize, based on our ChIP data, that MLL-AF9 up-regulates EVI1 transcription via H3K79 methylation, which is known to be a major gene regulatory mechanism used by some MLL-fusion proteins in leukemia. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML, MLL fusion protein in AML |
| + |
MECOM | up-regulates quantity by expression
transcriptional regulation
|
GATA2 |
0.368 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266062 |
|
|
Homo sapiens |
HEL Cell |
| pmid |
sentence |
| 15889140 |
Evi1 directly binds to the promoter region of GATA-2 and thus enhances the GATA-2 transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
MECOM
- 
- 