| + |
CARM1 | down-regulates activity 
methylation
|
RUNX1 |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261967 |
Arg223 |
PAPTPNPrASLNHST |
Homo sapiens |
Hematopoietic Stem Cell |
| pmid |
sentence |
| 24332853 |
We have found that PRMT4 is highly expressed in HSPCs, where it functions as an inhibitor of myeloid differentiation (Figure 7G). In these cells, PRMT4 methylates RUNX1 at R223, promoting the assembly of a DPF2-containing transcriptional co-repressive complex, and repressing transcription at the miR-223 locus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | up-regulates 
phosphorylation
|
RUNX1 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169318 |
Ser21 |
TPPSTALsPGKMSEA |
Homo sapiens |
|
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138908 |
Ser249 |
DTRQIQPsPPWSYDQ |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138912 |
Ser266 |
QYLGSIAsPSVHPAT |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
Phosphorylation of ser-48, ser-303, and ser-424 by cyclin-dependent kinases (cdks) increases runx1 trans-activation activity without perturbing p300 interaction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169322 |
Ser397 |
SMVGGERsPPRILPP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138920 |
Thr273 |
SPSVHPAtPISPGRA |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
Phosphorylation of ser-48, ser-303, and ser-424 by cyclin-dependent kinases (cdks) increases runx1 trans-activation activity without perturbing p300 interaction. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, KIT in AML |
| + |
CyclinB/CDK1 | up-regulates
phosphorylation
|
RUNX1 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216916 |
Ser21 |
TPPSTALsPGKMSEA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216912 |
Ser397 |
SMVGGERsPPRILPP |
Homo sapiens |
|
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CyclinD3/CDK6 | up-regulates activity
phosphorylation
|
RUNX1 |
0.562 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273031 |
Ser21 |
TPPSTALsPGKMSEA |
Homo sapiens |
|
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273029 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
|
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273030 |
Ser397 |
SMVGGERsPPRILPP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK6 | up-regulates
phosphorylation
|
RUNX1 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169326 |
Ser21 |
TPPSTALsPGKMSEA |
Homo sapiens |
|
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138953 |
Ser249 |
DTRQIQPsPPWSYDQ |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138957 |
Ser266 |
QYLGSIAsPSVHPAT |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169330 |
Ser397 |
SMVGGERsPPRILPP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138965 |
Thr273 |
SPSVHPAtPISPGRA |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML |
| + |
CDK2 | up-regulates activity
phosphorylation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138928 |
Ser249 |
DTRQIQPsPPWSYDQ |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138932 |
Ser266 |
QYLGSIAsPSVHPAT |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138936 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138940 |
Thr273 |
SPSVHPAtPISPGRA |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates quantity by destabilization
phosphorylation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268218 |
Ser249 |
DTRQIQPsPPWSYDQ |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268219 |
Ser266 |
QYLGSIAsPSVHPAT |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268221 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268220 |
Thr273 |
SPSVHPAtPISPGRA |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | up-regulates activity
phosphorylation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138969 |
Ser249 |
DTRQIQPsPPWSYDQ |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138973 |
Ser266 |
QYLGSIAsPSVHPAT |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138985 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138981 |
Thr273 |
SPSVHPAtPISPGRA |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | up-regulates
phosphorylation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244703 |
Ser249 |
DTRQIQPsPPWSYDQ |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244707 |
Ser266 |
QYLGSIAsPSVHPAT |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244715 |
Thr273 |
SPSVHPAtPISPGRA |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, NPM1_new |
| + |
CyclinA2/CDK2 | down-regulates activity
phosphorylation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217340 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
|
| pmid |
sentence |
| 17015473 |
Previous studies have shown that phosphorylation of aml1, particularly at serines 276 and 303, affects its transcriptional activation. Here, we report that phosphorylation of aml1 serines 276 and 303 can be blocked in vivo by inhibitors of the cyclin-dependent kinases (cdks) cdk1 and cdk2. Furthermore, these residues can be phosphorylated in vitro by purified cdk1/cyclin b and cdk2/cyclin a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK6 | up-regulates activity
phosphorylation
|
RUNX1 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169334 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
|
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138961 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML |
| + |
CDK2 | down-regulates activity
phosphorylation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149976 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
|
| pmid |
sentence |
| 17015473 |
Previous studies have shown that phosphorylation of aml1, particularly at serines 276 and 303, affects its transcriptional activation. Here, we report that phosphorylation of aml1 serines 276 and 303 can be blocked in vivo by inhibitors of the cyclin-dependent kinases (cdks) cdk1 and cdk2. Furthermore, these residues can be phosphorylated in vitro by purified cdk1/cyclin b and cdk2/cyclin a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | up-regulates activity
phosphorylation
|
RUNX1 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138916 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
Phosphorylation of ser-48, ser-303, and ser-424 by cyclin-dependent kinases (cdks) increases runx1 trans-activation activity without perturbing p300 interaction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, KIT in AML |
| + |
CDK1 | down-regulates quantity by destabilization
phosphorylation
|
RUNX1 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149972 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
|
| pmid |
sentence |
| 17015473 |
Aml1/runx1 phosphorylation by cyclin-dependent kinases regulates the degradation of aml1/runx1 by the anaphase-promoting complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, KIT in AML |
| + |
ERK1/2 | up-regulates activity
phosphorylation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244711 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, NPM1_new |
| + |
RUNX1 | down-regulates quantity by repression
transcriptional regulation
|
ANKRD26 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266069 |
|
|
Homo sapiens |
Megakaryocyte |
| pmid |
sentence |
| 24430186 |
In healthy individual, RUNX1/FLI1 complex negatively regulates ANKRD26 gene expression in MKs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUNX1 | up-regulates quantity by expression 
transcriptional regulation
|
KIT |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259133 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30500954 |
Notably, upregulation of c-KIT expression by FUBP1 and RUNX1 promotes cell proliferation and renders cells more resistant to the c-KIT inhibitor imatinib mesylate, a common therapeutic drug. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML, KIT in AML |
| + |
RUNX1 | down-regulates quantity by repression
transcriptional regulation
|
MYC |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260093 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29958106 |
RUNX1 represses MYC expression through direct binding at three downstream enhancer elements |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, miRNA in AML, MLL fusion protein in AML, NPM1_new |
| + |
CBFbeta-MYH11 | down-regulates activity
binding
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255743 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29958106 |
The genes encoding CBFβ and RUNX1 are frequent targets of mutations in hematologic malignancies. The chromosome inversion inv(16)(p13;q22), found in 8% of acute myeloid leukemia (AML) cases, fuses the CBFB and MYH11 genes to produce the leukemic oncoprotein CBFβ-SMMHC. This fusion protein has higher affinity and altered stoichiometry for RUNX1 relative to the native CBFβ (Cao et al., 1997; Lukasik et al., 2002). During development, CBFβ-SMMHC expression blocks definitive hematopoiesis and embryos die at mid-gestation (Castilla et al., 1996), a similar phenotype to that of Runx1- and Cbfb-knock out embryos (Wang et al., 1996a; Wang et al., 1996b), indicating that CBFβ-SMMHC has a dominant negative effect on RUNX function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML, KIT in AML |
| + |
FLT3 | up-regulates activity
|
RUNX1 |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256307 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28213513 |
Our finding that RUNX1 protein levels are dependent on FLT3-ITD signaling in AML cells and that, together, they synergize to generate AML. […]Our work demonstrated that Tyr phosphorylation within the ID region of RUNX1 is critical for its oncogenic potential, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, miRNA in AML, NPM1_new |
| + |
RUNX1 | form complex 
binding
|
Core Binding Factor complex |
0.841 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255710 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12495904 |
The core binding factor (CBF) transcription complex, consisting of the interacting proteins RUNX1 and CBFβ, is essential for normal hematopoiesis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MLL-AF9 | down-regulates quantity by repression 
transcriptional regulation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255851 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24449215 |
However, the functional consequence of MLL fusions on RUNX1/CBFβ activity has not been fully understood. In this report, we show that MLL fusion proteins and the N-terminal MLL portion of MLL fusions downregulate RUNX1 and CBFβ protein expression via the MLL CXXC domain and flanking regions. We found that MLL-BP and the 3 MLL fusion proteins all decreased RUNX1 levels, and MLL-eleven nineteen leukemia (ENL) caused a greater decrease in RUNX1 compared with MLL-AF9 and MLL-AF4 fusion proteins. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260128 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24449215 |
However, the functional consequence of MLL fusions on RUNX1/CBFβ activity has not been fully understood. In this report, we show that MLL fusion proteins and the N-terminal MLL portion of MLL fusions downregulate RUNX1 and CBFβ protein expression via the MLL CXXC domain and flanking regions. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, miRNA in AML, MLL fusion protein in AML |
| + |
RAD21 | down-regulates quantity by repression
transcriptional regulation
|
RUNX1 |
0.288 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259973 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24321385 |
We observed that depletion of RAD21 (but not CTCF) enhanced RUNX1 transcription in human HL-60 myelocytic leukemia cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML, NPM1_new |
| + |
CBFB | up-regulates quantity by stabilization
binding
|
RUNX1 |
0.841 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255712 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 11179217 |
We observed previously that the RUNX proteins are susceptible to proteolytic degradation (Ogawa et al., 1993b). In this study, we show that the ubiquitin‚proteasome system is largely responsible for this degradation. We also show that when PEBP2Œ≤ dimerizes with RUNX it inhibits the ubiquitylation of RUNX, which is necessary for the protein to be targeted for proteolysis by the proteasome. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255742 |
|
|
Mus musculus |
32D Clone3 Cell |
| pmid |
sentence |
| 11179217 |
The RUNX genes encode the α subunit of the transcription factor PEBP2/CBF. The β subunit consists of the non-RUNX protein PEBP2β. We found that RUNX1/AML1, which is essential for hematopoiesis, is continuously subjected to proteolytic degradation mediated by the ubiquitin–proteasome pathway. When PEBP2β is present, however, the ubiquitylation of RUNX1 is abrogated and this causes a dramatic inhibition of RUNX1 proteolysis. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| Pathways: | HaematopoiesisTranscriptionalControl |
| + |
YAP/TAZ | up-regulates activity
binding
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277664 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25287865 |
The WW domains are essential for YAP-induced cell proliferation (261) and mediate binding of YAP/TAZ to PPxY motif-containing transcription factors such as RUNX, p73, and the cytoplasmic domain of ERBB4 or with the transcriptional cofactor WBP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277669 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25287865 |
The WW domains are essential for YAP-induced cell proliferation (261) and mediate binding of YAP/TAZ to PPxY motif-containing transcription factors such as RUNX, p73, and the cytoplasmic domain of ERBB4 or with the transcriptional cofactor WBP2 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
RUNX1 | up-regulates quantity by expression
transcriptional regulation
|
CDKN2A |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255713 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12091906 |
AML1 binds to a six base pair DNA sequence (TGT/cGGT) that is present in many hematopoietic-specific genes.The p53 promoter does not contain any perfect AML1 DNA-binding sites (TGT/cGGT), but the human p14ARF promoter contains eight such sites (Fig. 1a), as well as multiple sites that match the broader consensus sequence (PyGPy/AGGT) or that have a single change from the consensus site.AML1 regulates the p14ARF promoter through an AML1 consensus DNA-binding site. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML, NPM1_new |
| + |
RUNX1 | up-regulates quantity by expression
transcriptional regulation
|
BAALC |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255077 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22493267 |
We show that BAALC overexpression occurs in the presence of the T allele of SNP rs62527607[GT], which creates a binding site for the activating RUNX1 transcription factor in the BAALC promoter region. The mechanism is demonstrated experimentally in vitro using luciferase reporter assays and electrophoretic mobility shift assay (EMSA) analysis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
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 |
| + |
ARID5B | up-regulates quantity by expression
transcriptional regulation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256159 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29326336 |
We also observed that ARID5B regulates the expression of four major components of the TAL1 complex (namely, TAL1,GATA3, RUNX1, and MYB) in Jurkat cells. Knockdown of ARID5B resulted in reductions of the H3K27ac signals at those enhancer loci (Supplemental Fig. S6E–H) and down-regulation of all four factors at the mRNA (Fig. 6E) and protein levels (Fig. 6F). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MLL-ENL | down-regulates quantity by repression
transcriptional regulation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260127 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24449215 |
However, the functional consequence of MLL fusions on RUNX1/CBFβ activity has not been fully understood. In this report, we show that MLL fusion proteins and the N-terminal MLL portion of MLL fusions downregulate RUNX1 and CBFβ protein expression via the MLL CXXC domain and flanking regions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255853 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24449215 |
However, the functional consequence of MLL fusions on RUNX1/CBFβ activity has not been fully understood. In this report, we show that MLL fusion proteins and the N-terminal MLL portion of MLL fusions downregulate RUNX1 and CBFβ protein expression via the MLL CXXC domain and flanking regions. We found that MLL-BP and the 3 MLL fusion proteins all decreased RUNX1 levels, and MLL-eleven nineteen leukemia (ENL) caused a greater decrease in RUNX1 compared with MLL-AF9 and MLL-AF4 fusion proteins. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, miRNA 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 |
| + |
RUNX1 | up-regulates quantity by expression
transcriptional regulation
|
SPI1 |
0.675 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255709 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 23817177 |
RUNX1 wild-type protein first binds to the PU.1 URE region and recruits the MLL complex to open up part of the compact chromatin structure. The partially relaxed chromatin allows the binding of another RUNX1 at the PU.1 promoter region to further distort compact DNA structure. The relaxed form of chromatin facilitates the accumulation of transcription factors and cofactors to initiate transcriptional activity. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, miRNA in AML, MLL fusion protein in AML, HaematopoiesisTranscriptionalControl |
| + |
RUNX1 | up-regulates quantity by expression
transcriptional regulation
|
hsa-mir-223 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255817 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25092144 |
We could show that STAT5 is involved in miR-155 induction. STAT5 knockdown in FLT3-ITD model systems reduced miR-155 expression in vitro and in vivo. In silico analyses predicted an STAT binding site in the miR-155 promoter. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, miRNA in AML |
| + |
KMT2A | up-regulates quantity by stabilization
binding
|
RUNX1 |
0.549 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255708 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23817177 |
RUNX1 wild-type protein first binds to the PU.1 URE region and recruits the MLL complex to open up part of the compact chromatin structure. The partially relaxed chromatin allows the binding of another RUNX1 at the PU.1 promoter region to further distort compact DNA structure. The relaxed form of chromatin facilitates the accumulation of transcription factors and cofactors to initiate transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255707 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 22012064 |
Similar to CBFβ, we show that MLL binds to AML1 abrogating its proteasome-dependent degradation.Furthermore, we demonstrate that MLL binds to a region of AML1 (that is conserved in AML2 and AML3) and increases AML1 (AML2 and AML3) protein levels |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | HaematopoiesisTranscriptionalControl |
| + |
RUNX1 | up-regulates
|
Differentiation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249631 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19334039 |
AML1/RUNX1 mutants play a central role in the pathogenesis of MDS/AML. Both AML1 mutants are initiating factors for MDS-genesis by inhibiting differentiation of hematopoietic stem cells, and Ni-type mutant requires acquisition of proliferation ability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, Onco-fusion proteins in AML, KIT in AML, miRNA in AML, MLL fusion protein in AML, HaematopoiesisTranscriptionalControl, NPM1_new |
| + |
RUNX1 | up-regulates quantity by expression
transcriptional regulation
|
BCR-ABL |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272145 |
|
|
Homo sapiens |
Chronic Myeloid Leukemia Cell Line |
| pmid |
sentence |
| 34902205 |
RUNX1 transactivates BCR-ABL1 expression in Philadelphia chromosome positive acute lymphoblastic leukemia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML |
| + |
MLL-AF4 | down-regulates quantity by repression
transcriptional regulation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255855 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24449215 |
However, the functional consequence of MLL fusions on RUNX1/CBFβ activity has not been fully understood. In this report, we show that MLL fusion proteins and the N-terminal MLL portion of MLL fusions downregulate RUNX1 and CBFβ protein expression via the MLL CXXC domain and flanking regions. We found that MLL-BP and the 3 MLL fusion proteins all decreased RUNX1 levels, and MLL-eleven nineteen leukemia (ENL) caused a greater decrease in RUNX1 compared with MLL-AF9 and MLL-AF4 fusion proteins. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260126 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24449215 |
However, the functional consequence of MLL fusions on RUNX1/CBFβ activity has not been fully understood. In this report, we show that MLL fusion proteins and the N-terminal MLL portion of MLL fusions downregulate RUNX1 and CBFβ protein expression via the MLL CXXC domain and flanking regions. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, miRNA in AML, MLL fusion protein in AML |
| + |
RUNX1 | up-regulates quantity by expression
transcriptional regulation
|
GP1BA |
0.376 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254195 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17725493 |
We and others have previously shown that RUNX1 and GATA-1 physically interact and cooperate in the activation of megakaryocytic promoters such as alpha IIb integrin and glycoprotein Ibalpha. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DPF2 | down-regulates activity
binding
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261966 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24332853 |
The interaction between RUNX1 and DPF2 is dependent on the RUNX1 methylation status |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUNX1 | up-regulates quantity
transcriptional regulation
|
HHEX |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256305 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28213513 |
We identified Hhex as a direct target of RUNX1 and FLT3-ITD stimulation and confirmed high HHEX expression in FLT3-ITD AMLs. HHEX could replace RUNX1 in cooperating with FLT3-ITD to induce AML. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML |
| + |
RUNX1 | up-regulates quantity by expression
transcriptional regulation
|
ELANE |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254553 |
|
|
Homo sapiens |
Bone Marrow Cell |
| pmid |
sentence |
| 14594802 |
We find that LEF-1 and CBFalpha co-activate ELA2 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUNX1 | up-regulates quantity by expression
transcriptional regulation
|
miR-155 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255800 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26910834 |
RUNX1high was positively associated with miR-155, miR-125a, miR-99b, miR-133a, miR-130a, miR-25 and miR-92a-1. MiR-155 was previously found to function as an oncogene in CN-AML |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, miRNA in AML |
| + |
KAT6A/KAT6B | up-regulates
binding
|
RUNX1 |
0.418 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217201 |
|
|
Homo sapiens |
Macrophage, Leukemia Cell, Monocyte |
| pmid |
sentence |
| 11742995 |
The activation domain of aml1 is required for its interaction with moz / moz activates aml1_mediated transcription |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SWI/SNF complex | up-regulates activity
binding
|
RUNX1 |
0.432 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261965 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20506188 |
Our findings indicate that RUNX1 interacts with the human SWI/SNF complex to control hematopoietic-specific gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KAT6A | up-regulates
binding
|
RUNX1 |
0.477 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113056 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11742995 |
The activation domain of aml1 is required for its interaction with moz / moz activates aml1_mediated transcription |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUNX1 | form complex
binding
|
ELF4/RUNX1 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66963 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 10207087 |
We readily detected an in vivo physical interaction between mef and aml1 proteins in kasumi-1 cells/ coexpression of mef and aml1b synergistically activates promoter function |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAD21 | down-regulates activity
relocalization
|
RUNX1 |
0.288 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261514 |
|
|
Homo sapiens |
Acute Myeloid Leukemia Cell |
| pmid |
sentence |
| 26607380 |
Large-scale AML genome re-sequencing efforts have identified novel recurrently mutated genes, including the members of the cohesin complex (RAD21, SMC3, SMC1A, and STAG2), implicated in the pathogenesis of this disease.Using ATAC-seq, we determined that mutant cohesin lead to a state of elevated chromatin accessibility and higher predicted binding at transcription factor binding sites for ERG, GATA2, and RUNX1. Moreover, using ChIP-Seq, we formally demonstrated increased binding of GATA2 and RUNX1 to these sites. Finally, we demonstrated that knockdown of these three TFs in human HSPC can revert the differentiation block induced by mutant cohesin. These results support a model in which mutant cohesin impairs hematopoietic differentiation and enforces stem cell programs through the modulation of ERG, GATA2, and RUNX1 chromatin accessibility, expression, and activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML, NPM1_new |
| + |
MLL Fusion | down-regulates quantity by repression
transcriptional regulation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260129 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24449215 |
However, the functional consequence of MLL fusions on RUNX1/CBFβ activity has not been fully understood. In this report, we show that MLL fusion proteins and the N-terminal MLL portion of MLL fusions downregulate RUNX1 and CBFβ protein expression via the MLL CXXC domain and flanking regions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML, MLL fusion protein in AML |
| + |
RUNX1 | up-regulates quantity by expression
transcriptional regulation
|
CCL3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251738 |
|
|
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 12771199 |
We show that RUNX1 can specifically bind to both RUNX sites but that only the proximal RUNX site is essential for PMA/ PHA stimulation of the MIP-1a promoter in Jurkat T-cells. We also show that the endogenous MIP-1a promoter is constitutively bound by RUNX1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUNX1 | up-regulates quantity by expression
transcriptional regulation
|
ITGA2B |
0.472 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254193 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17725493 |
We and others have previously shown that RUNX1 and GATA-1 physically interact and cooperate in the activation of megakaryocytic promoters such as alpha IIb integrin and glycoprotein Ibalpha. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NUP98-HOXA9 | up-regulates quantity by expression
transcriptional regulation
|
RUNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261499 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17442773 |
Over 102 cytoplasmic mRNAs were significantly altered in K562 myeloid leukemic cells transduced with NUP98‐HOXA9, 92 being increased and only 10 decreased. Runx1 is also upregulated in the NUP98‐HOXA9 transcriptosome and is a critical regulator of hematopoietic development and a frequent target for chromosomal translocation in leukemia |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUNX1 | down-regulates activity
binding
|
IKK-complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255690 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22021368 |
We found that AML1 inhibits NF-κB signaling through interaction with IκB kinase complex in the cytoplasm. Remarkably, AML1 mutants found in myeloid tumors lack the ability to inhibit NF-κB signaling, and human cases with AML1-related leukemia exhibits distinctly activated NF-κB signaling |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GATA1 | up-regulates activity
binding
|
RUNX1 |
0.629 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254194 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17725493 |
We and others have previously shown that RUNX1 and GATA-1 physically interact and cooperate in the activation of megakaryocytic promoters such as alpha IIb integrin and glycoprotein Ibalpha. In particular, we will elaborate on recent data which suggest that GATA-1 targets RUNX1 for modification, in particular phosphorylation by cyclin-dependent kinases. Furthermore, targeting of RUNX1 by GATA-1 for phosphorylation may convert RUNX1 from a repressor to an activator. This is a potential mechanism of transcriptional cooperation and may be an essential step in megakaryocytic differentiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | HaematopoiesisTranscriptionalControl |
3.0
RUNX1
- 
- 