| + |
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 |
| + |
CyclinD3/CDK6 | down-regulates activity 
phosphorylation
|
PKM |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273032 |
Ser37 |
MCRLDIDsPPITARN |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 28607489 |
Here, using human cancer cells and patient-derived xenografts in mice, we show that the cyclin D3–CDK6 kinase phosphorylates and inhibits the catalytic activity of two key enzymes in the glycolytic pathway, 6-phosphofructokinase and pyruvate kinase M2.|Phosphomimicking mutants of PFKP (S679E) or PKM2 (S37E) displayed decreased catalytic activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276453 |
Ser37 |
MCRLDIDsPPITARN |
Homo sapiens |
T-cell Acute Lymphoblastic Leukemia Cell |
| pmid |
sentence |
| 28607489 |
We show that the cyclin D3-CDK6 kinase phosphorylates and inhibits the catalytic activity of two key enzymes in the glycolytic pathway, 6-phosphofructokinase and pyruvate kinase M2. Phosphomimicking mutants of PFKP (S679E) or PKM2 (S37E) displayed decreased catalytic activity, which was not further affected by pre-incubation with cyclin D3-CDK6 (Extended Data Fig. 3a, b). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276454 |
Ser37 |
MCRLDIDsPPITARN |
Homo sapiens |
|
| pmid |
sentence |
| 28607489 |
We show that the cyclin D3-CDK6 kinase phosphorylates and inhibits the catalytic activity of two key enzymes in the glycolytic pathway, 6-phosphofructokinase and pyruvate kinase M2. Phosphomimicking mutants of PFKP (S679E) or PKM2 (S37E) displayed decreased catalytic activity, which was not further affected by pre-incubation with cyclin D3-CDK6 (Extended Data Fig. 3a, b). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CyclinD3/CDK6 | down-regulates quantity by destabilization
phosphorylation
|
CDC25A |
0.615 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277343 |
Ser40 |
ASAAGGLsPVTNLTV |
Homo sapiens |
A-431 Cell |
| pmid |
sentence |
| 28192398 |
We demonstrate that CyclinD-CDK4/CDK6 complexes mediate the phosphorylation of CDC25A on Ser40 during G1 and that these complexes directly phosphorylate this residue in vitro. Importantly, we also find that CyclinD1-CDK4 decreases CDC25A stability in a ßTrCP-dependent manner and that Ser40 and Ser88 phosphorylations contribute to this regulation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277341 |
Ser88 |
DSGFCLDsPGPLDSK |
Homo sapiens |
A-431 Cell |
| pmid |
sentence |
| 28192398 |
We demonstrate that CyclinD-CDK4/CDK6 complexes mediate the phosphorylation of CDC25A on Ser40 during G1 and that these complexes directly phosphorylate this residue in vitro. Importantly, we also find that CyclinD1-CDK4 decreases CDC25A stability in a ßTrCP-dependent manner and that Ser40 and Ser88 phosphorylations contribute to this regulation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CyclinD3/CDK6 | down-regulates activity
phosphorylation
|
PFKP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273033 |
Ser679 |
MQQGGAPsPFDRNFG |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 28607489 |
Here, using human cancer cells and patient-derived xenografts in mice, we show that the cyclin D3–CDK6 kinase phosphorylates and inhibits the catalytic activity of two key enzymes in the glycolytic pathway, 6-phosphofructokinase and pyruvate kinase M2.|Phosphomimicking mutants of PFKP (S679E) or PKM2 (S37E) displayed decreased catalytic activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinD3/CDK6 | down-regulates activity
phosphorylation
|
PFKM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276452 |
|
|
in vitro |
|
| pmid |
sentence |
| 28607489 |
In vitro kinase reactions revealed that all three PFK1 isoforms (PFKP, PFKL, PFKM) and PKM2 were phosphorylated by cyclin D3-CDK6 (Extended Data Fig. 2a–d, Supplementary Table 4). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CyclinD3/CDK6 | down-regulates activity
phosphorylation
|
PFKL |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276451 |
|
|
in vitro |
|
| pmid |
sentence |
| 28607489 |
In vitro kinase reactions revealed that all three PFK1 isoforms (PFKP, PFKL, PFKM) and PKM2 were phosphorylated by cyclin D3-CDK6 (Extended Data Fig. 2a–d, Supplementary Table 4). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CCND3 | form complex 
binding
|
CyclinD3/CDK6 |
0.933 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273027 |
|
|
|
|
| pmid |
sentence |
| 8114739 |
Here, we show that the human PLSTIRE gene product is a novel cyclin-dependent kinase, cdk6. The cdk6 kinase is associated with cyclins D1, D2, and D3 in lysates of human cells and is activated by coexpression with D-type cyclins in Sf9 insect cells. |
|
| Publications: |
1 |
| + |
CDK6 | form complex
binding
|
CyclinD3/CDK6 |
0.933 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273028 |
|
|
|
|
| pmid |
sentence |
| 8114739 |
Here, we show that the human PLSTIRE gene product is a novel cyclin-dependent kinase, cdk6. The cdk6 kinase is associated with cyclins D1, D2, and D3 in lysates of human cells and is activated by coexpression with D-type cyclins in Sf9 insect cells. |
|
| Publications: |
1 |
3.0
CyclinD3/CDK6
CPX-2013