| + |
CDK4 | down-regulates quantity by destabilization 
phosphorylation
|
GATA4 |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276317 |
Ser105 |
AYTPPPVsPRFSFPG |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21447557 |
Finally, CDK4 phosphorylated GATA4 directly, which promoted the degradation of GATA4 in cultured cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 |
phosphorylation
|
SMAD3 |
0.752 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250766 |
Ser204 |
NHSMDAGsPNLSPNP |
in vitro |
|
| pmid |
sentence |
| 15241418 |
Thus, we have shown that Smad3 is phosphorylated by CDK4 and CDK2. Mutation of its CDK phosphorylation sites increases its transcriptional activity and antiproliferative function. | Thr 8 and the four sites in the linker (Thr 178, Ser 203, Ser 207 and Ser 212). Each of the five sites was phosphorylated by both CDK4 and CDK2 in vitro, and only Thr 8, Thr 178 and Ser 212 were phosphorylated by CDK4 and CDK2 in vivo phosphorylated by both CDK4 and CDK2 in vitro, and only Thr 8, Thr 178 and Ser 212 were phosphorylated by CDK4 and CDK2 in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250767 |
Ser208 |
DAGSPNLsPNPMSPA |
in vitro |
|
| pmid |
sentence |
| 15241418 |
Thus, we have shown that Smad3 is phosphorylated by CDK4 and CDK2. Mutation of its CDK phosphorylation sites increases its transcriptional activity and antiproliferative function. | Thr 8 and the four sites in the linker (Thr 178, Ser 203, Ser 207 and Ser 212). Each of the five sites was phosphorylated by both CDK4 and CDK2 in vitro, and only Thr 8, Thr 178 and Ser 212 were phosphorylated by CDK4 and CDK2 in vivo phosphorylated by both CDK4 and CDK2 in vitro, and only Thr 8, Thr 178 and Ser 212 were phosphorylated by CDK4 and CDK2 in vivo. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | Pancreatic ductal adenocarcinoma (PDA) |
| + |
CDK4 | down-regulates
phosphorylation
|
RASSF1 |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159849 |
Ser207 |
TSVRRRTsFYLPKDA |
Homo sapiens |
|
| pmid |
sentence |
| 18071316 |
This skp2-dependent destruction of rassf1a requires phosphorylation of the latter on serine-203 by cyclin d-cyclin-dependent kinase 4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 | down-regulates activity
phosphorylation
|
SMAD3 |
0.752 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-232142 |
Ser213 |
NLSPNPMsPAHNNLD |
Homo sapiens |
|
| pmid |
sentence |
| 15241418 |
We have mapped CDK4 and CDK2 phosphorylation sites to Thr 8, Thr 178 and Ser 212 in Smad3. Mutation of the CDK phosphorylation sites increases Smad3 transcriptional activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182822 |
Thr179 |
PQSNIPEtPPPGYLS |
Homo sapiens |
|
| pmid |
sentence |
| 19114991 |
In the nucleus cdk2/4-mediated phosphorylation of smad3 occurs mostly at thr8, thr179, and ser213. Cdk-dependent phosphorylation of smad3 inhibits its transcriptional activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-232146 |
Thr179 |
PQSNIPEtPPPGYLS |
Homo sapiens |
|
| pmid |
sentence |
| 15241418 |
We have mapped CDK4 and CDK2 phosphorylation sites to Thr 8, Thr 178 and Ser 212 in Smad3. Mutation of the CDK phosphorylation sites increases Smad3 transcriptional activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-232138 |
Thr8 |
MSSILPFtPPIVKRL |
Homo sapiens |
|
| pmid |
sentence |
| 15241418 |
We have mapped CDK4 and CDK2 phosphorylation sites to Thr 8, Thr 178 and Ser 212 in Smad3. Mutation of the CDK phosphorylation sites increases Smad3 transcriptional activity |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | Pancreatic ductal adenocarcinoma (PDA) |
| + |
CDK4 | down-regulates
phosphorylation
|
SMAD3 |
0.752 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182979 |
Ser213 |
NLSPNPMsPAHNNLD |
Homo sapiens |
|
| pmid |
sentence |
| 19114991 |
In the nucleus cdk2/4-mediated phosphorylation of smad3 occurs mostly at thr8, thr179, and ser213. Cdk-dependent phosphorylation of smad3 inhibits its transcriptional activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182983 |
Thr8 |
MSSILPFtPPIVKRL |
Homo sapiens |
|
| pmid |
sentence |
| 19114991 |
In the nucleus cdk2/4-mediated phosphorylation of smad3 occurs mostly at thr8, thr179, and ser213. Cdk-dependent phosphorylation of smad3 inhibits its transcriptional activity |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Pancreatic ductal adenocarcinoma (PDA) |
| + |
CDK4 | down-regulates
phosphorylation
|
RB1 |
0.928 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135181 |
Ser249 |
AVIPINGsPRTPRRG |
Homo sapiens |
|
| pmid |
sentence |
| 15809340 |
Phosphorylated by cdk6 and cdk4, and subsequently by cdk2 at ser-567 in g1, thereby releasing e2f1 which is then able to activate cell growth. Here we show that although these cdks phosphorylate multiple residues in prb, they do so with different residue selectivities in vitro;thr821 and thr826 are preferentially phosphorylated by cdk6 and cdk4, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200483 |
Ser780 |
STRPPTLsPIPHIPR |
Homo sapiens |
|
| pmid |
sentence |
| 23336272 |
Cyclin d1 is known to activate cdk4, which then phosphorylates the rb protein, leading to cell cycle progression. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200487 |
Ser795 |
SPYKFPSsPLRIPGG |
Homo sapiens |
|
| pmid |
sentence |
| 23336272 |
Cyclin d1 is known to activate cdk4, which then phosphorylates the rb protein, leading to cell cycle progression. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135185 |
Ser811 |
IYISPLKsPYKISEG |
Homo sapiens |
|
| pmid |
sentence |
| 15809340 |
Phosphorylated by cdk6 and cdk4, and subsequently by cdk2 at ser-567 in g1, thereby releasing e2f1 which is then able to activate cell growth. Here we show that although these cdks phosphorylate multiple residues in prb, they do so with different residue selectivities in vitro;thr821 and thr826 are preferentially phosphorylated by cdk6 and cdk4, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47899 |
Thr826 |
LPTPTKMtPRSRILV |
Homo sapiens |
|
| pmid |
sentence |
| 9139732 |
We demonstrate that phosphorylation by either cdk2-cyclin a, which phosphorylates t821, or cdk4-cyclin d1, which phosphorylates threonine 826, can disable prb for subsequent binding of an lxcxe protein. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| Pathways: | Pancreatic ductal adenocarcinoma (PDA) |
| + |
CDK4 | up-regulates activity 
phosphorylation
|
TOB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273602 |
Ser254 |
PAPQSQLsPNAKEFV |
in vitro |
|
| pmid |
sentence |
| 32404348 |
Taken together, these observations strongly support the notion that several different CDK-cyclin complexes are involved in the phosphorylation of Tob2 at S254.A more detailed regulatory context of Tob2 phosphorylation at S254 is provided by our findings from mass-spec and in vitro kinase analyses that suggest connections to PP2B and PP2C phosphatases and CDK-cyclin complexes, particularly CDK1, CDK2, and CDK4 (Table 1; Supplemental Table S2).One possibility is that the phosphorylation of S254 helps stabilize the interaction of Tob2 with the Ccr4–Not complex, which could contribute to Tob2's ability to recruit the entire Ccr4–Not complex and thus further enhances deadenylation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CDK4 | up-regulates activity
phosphorylation
|
CELF1 |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262735 |
Ser302 |
TSSGSSPsSSSSNSV |
Mus musculus |
|
| pmid |
sentence |
| 16931514 |
These studies showed that both the increased levels of CUGBP1 and cdk4-mediated hyper-phosphorylation of CUGBP1 are involved in the age-associated induction of the CUGBP1-eIF2 complex. The CUGBP1-eIF2 complex is bound to C/EBPbeta mRNA in the liver of old animals, and this binding correlates with the increased amounts of liver-enriched activator protein and liver-enriched inhibitory protein. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CDK4 | down-regulates
phosphorylation
|
RUNX3 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185120 |
Ser356 |
SSSGGDRsPTRMLAS |
Homo sapiens |
|
| pmid |
sentence |
| 19351720 |
Our findings demonstrate that the cell cycle proteins cyclin d1 and cdk4 induce runx2 and runx3 phosphorylation, ubiquitylation and proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 | up-regulates activity
phosphorylation
|
KAT2A |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275494 |
Ser372 |
EEIYGANsPIWESGF |
|
|
| pmid |
sentence |
| 24870244 |
Activated cyclin D1-Cdk4 kinase phosphorylates and activates GCN5|GCN5 T272A/S372A (AA) phosphorylation by cyclin D1-CDK4 kinase is diminished compared to GCN5 wild-type (WT) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275495 |
Thr272 |
LNYWKLEtPAQFRQR |
|
|
| pmid |
sentence |
| 24870244 |
Activated cyclin D1-Cdk4 kinase phosphorylates and activates GCN5|GCN5 T272A/S372A (AA) phosphorylation by cyclin D1-CDK4 kinase is diminished compared to GCN5 wild-type (WT) |
|
| Publications: |
2 |
| + |
CDK4 | up-regulates
phosphorylation
|
FOXM1 |
0.615 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177251 |
Ser4 |
sPRRPLIL |
Homo sapiens |
|
| pmid |
sentence |
| 22094256 |
We identified the forkhead box m1 (foxm1) transcription factor as a common critical phosphorylation target. Cdk4/6 stabilize and activate foxm1these data identify five overlapping in vivo and in vitro cdk4/6 target sites in foxm1 (s4, s35, t611, t620 and t627) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177255 |
Thr611 |
ETLPISStPSKSVLP |
Homo sapiens |
|
| pmid |
sentence |
| 22094256 |
We identified the forkhead box m1 (foxm1) transcription factor as a common critical phosphorylation target. Cdk4/6 stabilize and activate foxm1these data identify five overlapping in vivo and in vitro cdk4/6 target sites in foxm1 (s4, s35, t611, t620 and t627) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177259 |
Thr620 |
SKSVLPRtPESWRLT |
Homo sapiens |
|
| pmid |
sentence |
| 22094256 |
We identified the forkhead box m1 (foxm1) transcription factor as a common critical phosphorylation target. Cdk4/6 stabilize and activate foxm1these data identify five overlapping in vivo and in vitro cdk4/6 target sites in foxm1 (s4, s35, t611, t620 and t627) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177263 |
Thr627 |
TPESWRLtPPAKVGG |
Homo sapiens |
|
| pmid |
sentence |
| 22094256 |
We identified the forkhead box m1 (foxm1) transcription factor as a common critical phosphorylation target. Cdk4/6 stabilize and activate foxm1these data identify five overlapping in vivo and in vitro cdk4/6 target sites in foxm1 (s4, s35, t611, t620 and t627) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177266 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22094256 |
We identified the forkhead box m1 (foxm1) transcription factor as a common critical phosphorylation target. Cdk4/6 stabilize and activate foxm1, thereby maintain expression of g1/s phase genes, suppress the levels of reactive oxygen species (ros), and protect cancer cells from senescence. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
CDK4 | up-regulates activity
phosphorylation
|
PAX3 |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278512 |
Ser430 |
TTVSASCsQRLDHMK |
Homo sapiens |
|
| pmid |
sentence |
| 23469153 |
In summary, our study showed that Cdk4 phosphorylates and activates PAX3-FOXO1, thereby promoting its oncogenic function.|These findings suggest that Cdk4 phosphorylates the Ser 430 residue of PAX3-FOXO1 in vitro . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 | up-regulates activity
phosphorylation
|
FOXO1 |
0.469 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278377 |
Ser430 |
KYTYGQSsMSPLPQM |
Homo sapiens |
|
| pmid |
sentence |
| 23469153 |
In summary, our study showed that Cdk4 phosphorylates and activates PAX3-FOXO1, thereby promoting its oncogenic function.|These findings suggest that Cdk4 phosphorylates the Ser 430 residue of PAX3-FOXO1 in vitro . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 | up-regulates
phosphorylation
|
PELP1 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167770 |
Ser477 |
ADALKLRsPRGSPDG |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20807815 |
Using site-directed mutagenesis and in vitro kinase assays, we identified ser(477) and ser(991) of pelp1 as cdk phosphorylation sites. we identified pelp1 as a novel substrate of cdks and found that cdk phosphorylation is important for the proper function of pelp1 in modulating hormone-driven cell cycle progression and also for optimal e2f transactivation function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167774 |
Ser991 |
PALPPPEsPPKVQPE |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20807815 |
Using site-directed mutagenesis and in vitro kinase assays, we identified ser(477) and ser(991) of pelp1 as cdk phosphorylation sites. we identified pelp1 as a novel substrate of cdks and found that cdk phosphorylation is important for the proper function of pelp1 in modulating hormone-driven cell cycle progression and also for optimal e2f transactivation function. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK4 | down-regulates
phosphorylation
|
BRCA1 |
0.657 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153450 |
Ser632 |
LVVSRNLsPPNCTEL |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17334399 |
In particular, we have identified ser 632 of brca1 as a cyclin d1/cdk4 phosphorylation site in vitro. Using chromatin immunoprecipitation assays, we observed that the inhibition of cyclin d1/cdk4 activity resulted in increased brca1 dna binding at particular promoters in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 | up-regulates activity
phosphorylation
|
RBL1 |
0.803 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250763 |
Ser650 |
SVHERYSsPTAGSAK |
Homo sapiens |
|
| pmid |
sentence |
| 12006580 |
Here we assessed the effects of alanine substitution at the individual or combined Cdk4(6)-specific sites in p130, compared with homologous sites in p107 (Thr(369)/Ser(650)/Ser(964)). In U-2-OS cells, the triple p107(DeltaCdk4)* mutant strongly inhibited E2F-4 activity and imposed a G(1) arrest resistant to cyclin D1 coexpression. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250764 |
Ser964 |
MMDAPPLsPFPHIKQ |
Homo sapiens |
|
| pmid |
sentence |
| 12006580 |
Here we assessed the effects of alanine substitution at the individual or combined Cdk4(6)-specific sites in p130, compared with homologous sites in p107 (Thr(369)/Ser(650)/Ser(964)). In U-2-OS cells, the triple p107(DeltaCdk4)* mutant strongly inhibited E2F-4 activity and imposed a G(1) arrest resistant to cyclin D1 coexpression. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250765 |
Thr369 |
KRSFAPStPLTGRRY |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12006580 |
Here we assessed the effects of alanine substitution at the individual or combined Cdk4(6)-specific sites in p130, compared with homologous sites in p107 (Thr(369)/Ser(650)/Ser(964)). In U-2-OS cells, the triple p107(DeltaCdk4)* mutant strongly inhibited E2F-4 activity and imposed a G(1) arrest resistant to cyclin D1 coexpression. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK7 | up-regulates
phosphorylation
|
CDK4 |
0.575 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36549 |
Thr172 |
YSYQMALtPVVVTLW |
Homo sapiens |
|
| pmid |
sentence |
| 8139570 |
Phosphorylation of cdk4 on threonine 172 by a cdk-activating kinase (cak). therefore, formation of the cyclin d-cdk4 complex and phosphorylation of the bound catalytic subunit are independently regulated, and in addition to the requirement for cak activity, serum stimulation is required to promote assembly of the complexes in mammalian cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAK complex | up-regulates
phosphorylation
|
CDK4 |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269329 |
Thr172 |
YSYQMALtPVVVTLW |
Homo sapiens |
|
| pmid |
sentence |
| 8139570 |
Phosphorylation of cdk4 on threonine 172 by a cdk-activating kinase (cak). therefore, formation of the cyclin d-cdk4 complex and phosphorylation of the bound catalytic subunit are independently regulated, and in addition to the requirement for cak activity, serum stimulation is required to promote assembly of the complexes in mammalian cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 | down-regulates
phosphorylation
|
PRDX1 |
0.227 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87105 |
Thr90 |
CHLAWVNtPKKQGGL |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11986303 |
Peroxiredoxin (prx) i is a member of the peroxiredoxin family of peroxidases and contains a consensus site (thr(90)-pro-lys-lys) for phosphorylation by cyclin-dependent kinases (cdks). This protein has now been shown to be phosphorylated specifically on thr(90) by several cdks, including cdc2, in vitro. Phosphorylation of prx i on thr(90) reduced the peroxidase activity of this protein by 80%.Prx i was also phosphorylated, with an efficiency similar to that observed with cdc2, when incubated in vitro with cdk2, cdk4, or cdk6 that had been immunoprecipitated from hela cell lysates with specific antibodies (data not shown). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YES1 | down-regulates
phosphorylation
|
CDK4 |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178624 |
Tyr17 |
AEIGVGAyGTVYKAR |
Homo sapiens |
|
| pmid |
sentence |
| 18479465 |
We purified tyrosine 17 kinases from hela cells and found that the src family non-receptor tyrosine kinase c-yes contributes a large fraction of the tyrosine 17 kinase activity in hela lysatesthis site is equivalent to tyrosine 15 of cyclin dependent kinase 1, which undergoes inhibitory phosphorylation by wee1 and myt1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC25A | up-regulates activity
dephosphorylation
|
CDK4 |
0.699 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277138 |
Tyr17 |
AEIGVGAyGTVYKAR |
Homo sapiens |
|
| pmid |
sentence |
| 27485204 |
Cdc25A mainly promotes G1-S transition by dephosphorylating CDK4 (Y17)-cyclin D, CDK6 (Y24)-cyclin D and CDK2 (T14 and Y15)-cyclin E/A complexes and G2-M progression by dephosphorylating CDK1 (T14 and Y15)-cyclin A/B .|Cdc25A mainly promotes G1-S transition by dephosphorylating CDK4 (Y17)-cyclin D, CDK6 (Y24)-cyclin D and CDK2 (T14/Y15)-cyclin E/A complexes and G2-M progression by dephosphorylating CDK1 (T14/Y15)-cyclin A/B . |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267568 |
Tyr17 |
AEIGVGAyGTVYKAR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23429262 |
Invalidation of CDK4 has no impact by itself on the cell proliferation, but invalidation of CDC25A prevents the dephosphorylation of CDK6 (Y24) and CDK4 (Y17) residues, and impedes their association with CCNDs. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
4-(2,6-dichlorobenzamido)-N-(piperidin-4-yl)-pyrazole-3-carboxamide | down-regulates activity
chemical inhibition
|
CDK4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262221 |
|
|
in vitro |
|
| pmid |
sentence |
| 29901072 |
AT7519, a pyrazole 3-carboxyamide compound, was developed by Astex and acts as an inhibitor of CDK1, CDK2, CDK4, CDK6 and CDK9. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262220 |
|
|
in vitro |
|
| pmid |
sentence |
| 29901072 |
AT7519, a pyrazole 3-carboxyamide compound, was developed by Astex and acts as an inhibitor of CDK1, CDK2, CDK4, CDK6 and CDK9. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CDKN2C | down-regulates
binding
|
CDK4 |
0.868 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-44598 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8891723 |
The first group, including p16ink4a, p15ink4b,p18ink4cand p19ink4d, is specific for the g1 cdks,cdk4and cdk6, inhibiting the kinase activity of cyclin d/cdk4-cdk6 complexes on prb. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 | down-regulates
binding
|
MYOG |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176530 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21902831 |
In contrast to cdk2, cyclin d/cdk4 blocks myod activity through an as yet unclear mechanism that may involve direct binding. Cyclin d/cdk4 can also block the activity of myogenin and all mef2 isoforms. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCND1 | up-regulates
binding
|
CDK4 |
0.964 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201666 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 23562856 |
D-type cyclins (cyclin d1, d2, or d3) and their associated cyclin-dependent kinases (cdk4, cdk6) connect signals from cytokines to the cell cycle machinery, and they propel cells through the g1 restriction point and into the s phase when activated by cyclin d1, cdk4 is able to phosphorylate prb, |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-32295 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7736585 |
D-type cyclins (cyclin d1, d2, or d3) and their associated cyclin-dependent kinases (cdk4, cdk6) connect signals from cytokines to the cell cycle machinery, and they propel cells through the g1 restriction point and into the s phase when activated by cyclin d1, cdk4 is able to phosphorylate prb, |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
R547 | down-regulates
chemical inhibition
|
CDK4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206364 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MYC | up-regulates quantity by expression
transcriptional regulation
|
CDK4 |
0.581 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102734 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12835716 |
C-myc directly activates transcription of cyclin d1, cyclin d2 and cdk4, and leads to cdk 4/6 activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
palbociclib | down-regulates
chemical inhibition
|
CDK4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205704 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 | down-regulates
binding,
|
MEF2C |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176518 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21902831 |
In contrast to cdk2, cyclin d/cdk4 blocks myod activity through an as yet unclear mechanism that may involve direct binding. Cyclin d/cdk4 can also block the activity of myogenin and all mef2 isoforms. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176521 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21902831 |
Not much is known about how this occurs, but inhibition of mef2c by cdk4 prevents the association of mef2 with its transcriptional coactivator, glucocorticoid receptor-interacting protein 1 (grip1). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
alvocidib hydrochloride | down-regulates
chemical inhibition
|
CDK4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192464 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDKN2A | down-regulates
binding
|
CDK4 |
0.903 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-44554 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8891723 |
The first group, including p16ink4a, p15ink4b,p18ink4cand p19ink4d, is specific for the g1 cdks, cdk4 and cdk6, inhibiting the kinase activity of cyclin d/cdk4-cdk6 complexes on prb. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140409 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16161044 |
The cdk-inhibitor p16 is a tumor suppressor gene that is inactivated in many forms of cancer. In addition, cytoplasmic p16 bound cyclin dependent kinase (cdk)4/6, potentially indicating that p16 could have a function in the cytoplasm. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Pancreatic ductal adenocarcinoma (PDA) |
| + |
CDKN2B | down-regulates
binding
|
CDK4 |
0.876 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-46758 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9042862 |
We present evidence that the different subcellular location of p15 and p27 ensures the prior access of p15 to cdk4. In the cell, p15 is localized mostly in the cytoplasm, whereas p27 is nuclear. p15 prevails over p27 or a p27 construct consisting of the cdk inhibitory domain tagged with a nuclear localization signal. However, when p15 and p27 are forced to reside in the same subcellular location, either the cytoplasm or the nucleus, p15 no longer prevents p27 from binding to cdk4. These properties allow p15 and p27 to coordinately inhibit cdk4 and cdk2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Lung |
| Pathways: | Pancreatic ductal adenocarcinoma (PDA) |
| + |
alvocidib | down-regulates activity
chemical inhibition
|
CDK4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258172 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
alvocidib | down-regulates
chemical inhibition
|
CDK4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192038 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
R547 | down-regulates activity
chemical inhibition
|
CDK4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259794 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258274 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
4-(2,6-dichlorobenzamido)-N-(piperidin-4-yl)-pyrazole-3-carboxamide | down-regulates
chemical inhibition
|
CDK4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189990 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LRRC4 | down-regulates quantity by repression 
transcriptional regulation
|
CDK4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264059 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25526788 |
LRRC4/NGL-2 can delay the cell cycle in late G1 by increasing the expression of cell cycle inhibitory molecules (p21, p27) and reducing the expression of cell cycle regulatory proteins (CyclinD1, CDK2, CyclinE, CDK4) via the inhibition of K-Ras/c-Raf/ERK/MAPK, PI-3K/AKT/NF- κB, p70S6/PKC and STAT3, and the upregulation of the JNK2/c-Jun/mp53 signaling pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
CDK4 | down-regulates
binding
|
MEF2D |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176524 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21902831 |
In contrast to cdk2, cyclin d/cdk4 blocks myod activity through an as yet unclear mechanism that may involve direct binding. Cyclin d/cdk4 can also block the activity of myogenin and all mef2 isoforms. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDKN1A | down-regulates
binding
|
CDK4 |
0.94 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-29957 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7626805 |
P21cip1 is a cyclin-dependent kinase (cdk) inhibitor that is transcriptionally activated by p53 in response to dna damage.We Have explored the interaction of p21 with the currently known cdks. p21 effectively inhibits cdk2, cdk3, cdk4, and cdk6 kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 | down-regulates
binding
|
MEF2A |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176515 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21902831 |
In contrast to cdk2, cyclin d/cdk4 blocks myod activity through an as yet unclear mechanism that may involve direct binding. Cyclin d/cdk4 can also block the activity of myogenin and all mef2 isoforms. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TGFB1 | down-regulates quantity by repression
transcriptional regulation
|
CDK4 |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-39045 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8402878 |
Here we show that tgf beta 1 induces suppression of cdk4 synthesis in g1 in mink lung epithelial cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Lung |
| + |
CDK4 | down-regulates
binding
|
MYOD1 |
0.521 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176527 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21902831 |
In contrast to cdk2, cyclin d/cdk4 blocks myod activity through an as yet unclear mechanism that may involve direct binding. Cyclin d/cdk4 can also block the activity of myogenin and all mef2 isoforms. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-[6,6-dimethyl-5-[(1-methyl-4-piperidinyl)-oxomethyl]-1,4-dihydropyrrolo[3,4-c]pyrazol-3-yl]-3-methylbutanamide | down-regulates
chemical inhibition
|
CDK4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206130 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 | form complex 
binding
|
CyclinD/CDK4 |
0.964 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-32301 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7736585 |
D-type cyclins (cyclin d1, d2, or d3) and their associated cyclin-dependent kinases (cdk4, cdk6) connect signals from cytokines to the cell cycle machinery, and they propel cells through the g1 restriction point and into the s phase when activated by cyclin d1, cdk4 is able to phosphorylate prb, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pancreatic ductal adenocarcinoma (PDA) |
3.0
CDK4
- 
- 