| + |
DYRK1B | up-regulates 
phosphorylation
|
CDKN1B |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235805 |
Ser10 |
NVRVSNGsPSLERMD |
Mus musculus |
|
| pmid |
sentence |
| 15546868 |
Mirk phosphorylates p27 at ser-10, thus stabilizing p27 and blocking its nuclear export and degradation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CDK16 | down-regulates quantity 
phosphorylation
|
CDKN1B |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278214 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
|
| pmid |
sentence |
| 25205104 |
Experimentally overexpressing PCTAIRE1 in these cells caused p27 Ser10 phosphorylation , and reduced p27 protein levels in a proteasome dependent manner .|PCTAIRE1 phosphorylates p27 at Ser 10. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UHMK1 | up-regulates
phosphorylation
|
CDKN1B |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90274 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
|
| pmid |
sentence |
| 12093740 |
Hkis is a nuclear protein that binds the c-terminal domain of p27(kip1) and phosphorylates it on s10 in vitro and in vivo, promoting its nuclear export to the cytoplasm.Phosphorylation at serine 10, a major phosphorylation site of p27(kip1), increases its protein stability |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-77705 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
|
| pmid |
sentence |
| 10831586 |
Hkis is a nuclear protein that binds the c-terminal domain of p27(kip1) and phosphorylates it on s10 in vitro and in vivo, promoting its nuclear export to the cytoplasm.Phosphorylation at serine 10, a major phosphorylation site of p27(kip1), increases its protein stability |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
HIPK2 | up-regulates
phosphorylation
|
CDKN1B |
0.254 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174617 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
|
| pmid |
sentence |
| 21715331 |
Homeodomain-interacting protein kinase-2 stabilizes p27(kip1) by its phosphorylation at serine 10 and contributes to cell motility |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
MAPK1 | up-regulates
phosphorylation
|
CDKN1B |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-77651 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
|
| pmid |
sentence |
| 10831586 |
Phosphorylation on ser-10 of kip1 is the major site of phosphorylation in resting cells, takes place at the g(0)-g1 phase and leads to protein stability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-77655 |
Ser178 |
EENVSDGsPNAGSVE |
Homo sapiens |
|
| pmid |
sentence |
| 10831586 |
Indeed, p27kip1 was phosphorylated by p42 mapk (erk2) in vitrothese results suggest that ser(10) is the major site of phosphorylation of p27(kip1) and that phosphorylation at this site, like that at thr(187), contributes to regulation of p27(kip1) stability. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | up-regulates
phosphorylation
|
CDKN1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244622 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
|
| pmid |
sentence |
| 10831586 |
Phosphorylation on ser-10 of kip1 is the major site of phosphorylation in resting cells, takes place at the g(0)-g1 phase and leads to protein stability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244517 |
Ser178 |
EENVSDGsPNAGSVE |
Homo sapiens |
|
| pmid |
sentence |
| 10831586 |
Indeed, p27kip1 was phosphorylated by p42 mapk (erk2) in vitrothese results suggest that ser(10) is the major site of phosphorylation of p27(kip1) and that phosphorylation at this site, like that at thr(187), contributes to regulation of p27(kip1) stability. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Integrin Signaling |
| + |
CDK16 | down-regulates quantity by destabilization
phosphorylation
|
CDKN1B |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273016 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25205104 |
In vitro kinase assays showed PCTAIRE1 phosphorylates p27 at Ser10. PCTAIRE1 silencing modulated Ser10 phosphorylation on p27 and led to its accumulation in cancer cells but not in nontransformed cells.|Together our findings reveal an unexpected role for PCTAIRE1 in regulating p27 stability, mitosis, and tumor growth, suggesting PCTAIRE1 as a candidate cancer therapeutic target. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | up-regulates activity
phosphorylation
|
CDKN1B |
0.332 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278250 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
|
| pmid |
sentence |
| 24806449 |
DYRK1A phosphorylates p27 Kip1 at Ser10 in primary neurons and in vivo.|Thus, our results identify DYRK1A as the predominant kinase that phosphorylates and stabilizes p27Kip1 during neuronal differentiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinY/CDK16 | down-regulates quantity by destabilization
phosphorylation
|
CDKN1B |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273012 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25205104 |
In vitro kinase assays showed PCTAIRE1 phosphorylates p27 at Ser10. PCTAIRE1 silencing modulated Ser10 phosphorylation on p27 and led to its accumulation in cancer cells but not in nontransformed cells.|Together our findings reveal an unexpected role for PCTAIRE1 in regulating p27 stability, mitosis, and tumor growth, suggesting PCTAIRE1 as a candidate cancer therapeutic target. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK6 | up-regulates
phosphorylation
|
CDKN1B |
0.855 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140401 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
|
| pmid |
sentence |
| 16160006 |
Phosphorylation on ser-10 is the major site of phosphorylation in resting cells, takes place at the g(0)-g1 phase and leads to protein stability.p27(kip1) was phosphorylated by v-cyclin-cdk6 predominantly on ser10, which enhances its cytoplasmic localization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
PPM1D | down-regulates activity
dephosphorylation
|
CDKN1B |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277109 |
Ser140 |
PKTDPSDsQTGLAEQ |
Homo sapiens |
|
| pmid |
sentence |
| 31959038 |
Increased expression of wildtype WIP1 reduces stability of p27 Kip1 while increased expression of similar amounts of phosphatase-dead WIP1 has no effect on p27 Kip1 protein stability.|We demonstrate that wildtype, but not phosphatase-dead WIP1, efficiently dephosphorylates p27 Kip1 Ser140 both in vitro and in cells and that this dephosphorylation is sensitive to the WIP1 specific inhibitor GSK 2830371. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHUK | down-regulates activity
phosphorylation
|
CDKN1B |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278438 |
Ser183 |
DGSPNAGsVEQTPKK |
Homo sapiens |
|
| pmid |
sentence |
| 23602409 |
Reduced nuclear p27 was also found in MCF7 human breast cancer cells that were transiently transfected with an IKKalpha expression vector; increased IKKalpha expression resulted in a dose dependent decrease in nuclear p27 and increased cytoplasmic p27 (XREF_FIG).|We found that IKKalpha phosphorylates p27 at S183 to cause its nuclear export. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 | down-regulates
phosphorylation, binding
|
CDKN1B |
0.85 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179109 |
Thr157 |
GIRKRPAtDDSSTQN |
Homo sapiens |
|
| pmid |
sentence |
| 18570873 |
Mtor may promote g1 progression in part through sgk1 activation and deregulate the cell cycle in cancers through both akt- and sgk-mediated p27 t157 phosphorylation and cytoplasmic p27 mislocalization. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88294 |
Thr198 |
PGLRRRQt |
Homo sapiens |
|
| pmid |
sentence |
| 12042314 |
Because Thr198-phosphorylated p27Kip1 was localized only in the cytoplasm, Akt might promote 14-3-3 binding to p27Kip1 by phosphorylation at Thr198, allowing its cytoplasmic localization and degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121944 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14967450 |
Furthermore, akt promotes cell cycle progression through downregulation of the cyclin dependent kinase inhibitor p27kip1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252534 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23400686 |
Furthermore, akt promotes cell cycle progression through downregulation of the cyclin dependent kinase inhibitor p27kip1. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
CDKN1B |
0.528 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93122 |
Thr157 |
GIRKRPAtDDSSTQN |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12244303 |
Akt-induced t157 phosphorylation causes retention of p27(kip1) in the cytoplasm, precluding p27(kip1)-induced g1 arrest.[__]Thus, cytoplasmic relocalization of p27(kip1), secondary to akt-mediated phosphorylation, is a novel mechanism whereby the growth inhibitory properties of p27(kip1) are functionally inactivated and the proliferation of breast cancer cells is sustained. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates
phosphorylation
|
CDKN1B |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179117 |
Thr157 |
GIRKRPAtDDSSTQN |
Homo sapiens |
|
| pmid |
sentence |
| 18570873 |
Activated sgk1 and p27 phosphorylation at t157, and both were inhibited by short-term rapamycin treatment and by sgk1 shrna. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK1 | up-regulates activity
phosphorylation
|
CDKN1B |
0.305 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261195 |
Thr157 |
GIRKRPAtDDSSTQN |
Mus musculus |
|
| pmid |
sentence |
| 23707388 |
We also demonstrate that i) CaMKI phosphorylates p27 at Thr157and Thr198 in human cells and at Thr170and Thr197in mouse cells to modulate its subcellular localization; |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261194 |
Thr198 |
PGLRRRQt |
Mus musculus |
|
| pmid |
sentence |
| 23707388 |
We also demonstrate that i) CaMKI phosphorylates p27 at Thr157and Thr198 in human cells and at Thr170and Thr197in mouse cells to modulate its subcellular localization;|Collectively, these results suggest that CaMKI is involved in mediating G1 progression by promoting cyclin D1/cdk4 complex formation through site-specific p27 phosphorylation in human lung epithelia. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
PIM | down-regulates
phosphorylation
|
CDKN1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259426 |
Thr157 |
GIRKRPAtDDSSTQN |
Homo sapiens |
|
| pmid |
sentence |
| 18593906 |
We show, herein, that all the pim family members (pim1, pim2, and pim3) bind to and directly phosphorylate the cyclin-dependent kinase inhibitor p27(kip1) at threonine-157 and threonine-198 residues in cells and in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
AKT | down-regulates activity
phosphorylation
|
CDKN1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244202 |
Thr157 |
GIRKRPAtDDSSTQN |
Homo sapiens |
|
| pmid |
sentence |
| 18570873 |
Mtor may promote g1 progression in part through sgk1 activation and deregulate the cell cycle in cancers through both akt- and sgk-mediated p27 t157 phosphorylation and cytoplasmic p27 mislocalization. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244194 |
Thr198 |
PGLRRRQt |
Homo sapiens |
|
| pmid |
sentence |
| 12042314 |
Because Thr198-phosphorylated p27Kip1 was localized only in the cytoplasm, Akt might promote 14-3-3 binding to p27Kip1 by phosphorylation at Thr198, allowing its cytoplasmic localization and degradation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Integrin Signaling |
| + |
PIM1 | down-regulates
phosphorylation
|
CDKN1B |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179296 |
Thr157 |
GIRKRPAtDDSSTQN |
Homo sapiens |
|
| pmid |
sentence |
| 18593906 |
We show, herein, that all the pim family members (pim1, pim2, and pim3) bind to and directly phosphorylate the cyclin-dependent kinase inhibitor p27(kip1) at threonine-157 and threonine-198 residues in cells and in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
CDK6 | down-regulates
phosphorylation
|
CDKN1B |
0.855 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140405 |
Thr187 |
NAGSVEQtPKKPGLR |
Homo sapiens |
B-lymphocyte, Lymphoma Cell |
| pmid |
sentence |
| 16160006 |
Phosphorylation on thr-187, by cdk2 leads to protein ubiquitination and proteasomal degradationp27(kip1) was phosphorylated by v-cyclin-cdk6 predominantly on ser10, which enhances its cytoplasmic localization. Interestingly, upon reactivation of kshv lytic cycle, v-cyclin-cdk6 phosphorylated p27(kip1) on thr187, which resulted in down-regulation of p27(kip1) protein levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
CDK1 | down-regulates
phosphorylation
|
CDKN1B |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-80230 |
Thr187 |
NAGSVEQtPKKPGLR |
Homo sapiens |
|
| pmid |
sentence |
| 10931950 |
Phosphorylation of kip1 on thr-187, by cdk1 and cdk2 leads to protein ubiquitination and proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, IDH-TET in AML |
| + |
MAPK3 | down-regulates
phosphorylation
|
CDKN1B |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-80234 |
Thr187 |
NAGSVEQtPKKPGLR |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10931950 |
These data suggest that increased signaling by erbb receptors up-regulates mapk activity, which, in turn, phosphorylates and destabilizes p27, thus contributing to dysregulated cell cycle progression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK2 | down-regulates
phosphorylation
|
CDKN1B |
0.951 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154188 |
Thr187 |
NAGSVEQtPKKPGLR |
Homo sapiens |
|
| pmid |
sentence |
| 17409098 |
Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. Here we provide evidence suggesting that both cdk2/e and phosphorylation of thr(187) on p27 are essential for the recognition of p27 by the scf(skp2/cks1) complex, the ubiquitin-protein isopeptide ligase (e3). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK8 | down-regulates
phosphorylation
|
CDKN1B |
0.289 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278513 |
Thr187 |
NAGSVEQtPKKPGLR |
Homo sapiens |
|
| pmid |
sentence |
| 25818643 |
As a consequence, CDK8 overexpression promoted p27 degradation, whereas CDK8 knockdown reduced it.|We also show that CDK8 promotes phosphorylation of p27 at T187 and then induces p27 ubiquitination and degradation in a Skp2-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA1 | up-regulates quantity by stabilization
phosphorylation
|
CDKN1B |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259859 |
Thr198 |
PGLRRRQt |
Mus musculus |
|
| pmid |
sentence |
| 30033086 |
P27Kip1-Mediated Cell Survival Is Dependent on AMPK-Specific Thr198 Phosphorylation|AMPK-dependent phosphorylation of p27Kip1 on Thr198 promotes p27Kip1 protein stability, resulting in more autophagy and less apoptosis. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PIM | down-regulates activity
phosphorylation
|
CDKN1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259425 |
Thr198 |
PGLRRRQt |
Homo sapiens |
|
| pmid |
sentence |
| 18593906 |
We show, herein, that all the pim family members (pim1, pim2, and pim3) bind to and directly phosphorylate the cyclin-dependent kinase inhibitor p27(kip1) at threonine-157 and threonine-198 residues in cells and in vitro.|Pim kinases promote cell cycle progression and tumorigenesis by down-regulating p27(Kip1) expression at both transcriptional and posttranslational levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
SGK1 | down-regulates activity
phosphorylation
|
CDKN1B |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179121 |
Thr198 |
PGLRRRQt |
Homo sapiens |
|
| pmid |
sentence |
| 18570873 |
Activated sgk1 and p27 phosphorylation at t157, and both were inhibited by short-term rapamycin treatment and by sgk1 shrna.|Akt acts downstream of PI3K to phosphorylate p27 at T157 and T198, leading to impaired nuclear p27 import, p27 accumulation in the cytoplasm, and loss of cyclin E-Cdk2 inhibition |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1G | up-regulates activity
dephosphorylation
|
CDKN1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277112 |
Thr198 |
PGLRRRQt |
Homo sapiens |
|
| pmid |
sentence |
| 27822412 |
By using genomic phosphatase screening, we identified a PPM family phosphatase, PPM1G, which could reduce p27 phosphorylation at T198.|Functionally, ectopic expression of PPM1G enhanced p27 protein stability and delayed cell cycle progression from G1 to S phase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIM1 | down-regulates activity
phosphorylation
|
CDKN1B |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179300 |
Thr198 |
PGLRRRQt |
Homo sapiens |
|
| pmid |
sentence |
| 18593906 |
We show, herein, that all the pim family members (pim1, pim2, and pim3) bind to and directly phosphorylate the cyclin-dependent kinase inhibitor p27(kip1) at threonine-157 and threonine-198 residues in cells and in vitro.|Pim kinases promote cell cycle progression and tumorigenesis by down-regulating p27(Kip1) expression at both transcriptional and posttranslational levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
SRC | down-regulates
phosphorylation
|
CDKN1B |
0.498 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152831 |
Tyr74 |
HKPLEGKyEWQEVEK |
Homo sapiens |
|
| pmid |
sentence |
| 17254967 |
Src regulates p27 stability through phosphorylation of p27 at tyrosine 74 and tyrosine 88. Our data indicate that phosphorylation by src impairs the cdk2 inhibitory action of p27 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152835 |
Tyr88 |
KGSLPEFyYRPPRPP |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17254967 |
Src regulates p27 stability through phosphorylation of p27 at tyrosine 74 and tyrosine 88. Our data indicate that phosphorylation by src impairs the cdk2 inhibitory action of p27 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152839 |
Tyr89 |
GSLPEFYyRPPRPPK |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17254967 |
Src regulates p27 stability through phosphorylation of p27 at tyrosine 74 and tyrosine 88. Our data indicate that phosphorylation by src impairs the cdk2 inhibitory action of p27 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
ABL1 | down-regulates quantity
phosphorylation
|
CDKN1B |
0.594 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245293 |
Tyr88 |
KGSLPEFyYRPPRPP |
Homo sapiens |
HEK-293 Cell, HeLa Cell |
| pmid |
sentence |
| 17254966 |
A conserved tyrosine residue (Y88) in the Cdk-binding domain of p27 can be phosphorylated by the Src-family kinase Lyn and the oncogene product BCR-ABL |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
JAK2 | down-regulates activity
phosphorylation
|
CDKN1B |
0.695 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278260 |
Tyr88 |
KGSLPEFyYRPPRPP |
Homo sapiens |
|
| pmid |
sentence |
| 21423214 |
JAK2 phosphorylates tyrosine residue 88 (Y88) of p27(Kip1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
ABL1 | down-regulates activity
phosphorylation
|
CDKN1B |
0.594 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251426 |
Tyr88 |
KGSLPEFyYRPPRPP |
in vitro |
|
| pmid |
sentence |
| 17254966 |
Lyn and Abl phosphorylate Y88 of p27 in vitro. phosphorylation of Y88 in p27 impaired its ability to inhibit the bound kinase complex |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
FLT3 | down-regulates activity
phosphorylation
|
CDKN1B |
0.29 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269208 |
Tyr88 |
KGSLPEFyYRPPRPP |
Mus musculus |
BA/F3 Cell |
| pmid |
sentence |
| 28522571 |
FLT3 and FLT3-ITD phosphorylate and inactivate the cyclin-dependent kinase inhibitor p27 Kip1 in acute myeloid leukemia|P27Kip1 (p27) can prevent cell proliferation by inactivating cyclin-dependent kinases. This function is impaired upon phosphorylation of p27 at tyrosine residue 88. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia |
| + |
LYN | down-regulates
phosphorylation
|
CDKN1B |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172904 |
Tyr88 |
KGSLPEFyYRPPRPP |
Homo sapiens |
|
| pmid |
sentence |
| 21423214 |
We previously reported that y88 phosphorylation of p27(kip1) by oncogenic tyrosine kinases impairs p27(kip1)-mediated cdk inhibition, and initiates its ubiquitin-dependent proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDKN1B | down-regulates
binding
|
CDK2 |
0.951 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154191 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17409098 |
P27, an important cell cycle regulator, blocks the g(1)/s transition in cells by binding and inhibiting cdk2/cyclin a and cdk2/cyclin e complexes (cdk2/e). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-SKP2 | down-regulates quantity by destabilization
polyubiquitination, ubiquitination
|
CDKN1B |
0.694 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272933 |
|
|
in vitro |
|
| pmid |
sentence |
| 10375532 |
Isolated SCF(Skp2) contained an E3 ubiquitin ligase activity towards p27. Our data thus suggest that SCF(Skp2) specifically targets p27 for degradation during cell-cycle progression.Immunodepletion of components of the complex - Cul-1, Skp1, or Skp2 - from the extract abolished p27 degradation, while addition of purified SCF(Skp2) to Skp2- depleted extract restored the capacity to degrade p27. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267557 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10559916 |
SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27|We conclude that the stable interaction of p27 with SKP2 is highly specific and dependent upon phosphorylation of p27 on T187. |
|
| Publications: |
2 |
Organism: |
In Vitro, Homo Sapiens |
| + |
PTPN11 | up-regulates activity
dephosphorylation
|
CDKN1B |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277168 |
|
|
in vitro |
|
| pmid |
sentence |
| 19066472 |
Moreover, SHP-2 was strongly activated on G-CSF stimulation and specifically dephosphorylated p27(Kip1) in vitro.|Most importantly, we could illustrate that SHP-2 modulates p27 (Kip1) stability and contributes to p27 (Kip1)-mediated cell cycle progression. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Acute Myeloid Leukemia |
| + |
MYC | down-regulates quantity by repression 
transcriptional regulation
|
CDKN1B |
0.534 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107032 |
|
|
Homo sapiens |
Breast Cancer Cell, T-lymphocyte |
| pmid |
sentence |
| 11313917 |
P27(kip1) gene is a target of transcriptional repression by c-myc. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| Pathways: | Acute Myeloid Leukemia, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition |
| + |
FOXO | up-regulates quantity
transcriptional regulation
|
CDKN1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252928 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 10783894 |
AFX transcriptionally activates p27kip1, resulting in increased protein levels. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, IDH-TET in AML |
| + |
RNF7 | down-regulates activity
ubiquitination
|
CDKN1B |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271447 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23136067 |
SAG (Sensitive to Apoptosis Gene), also known as RBX2 (RING box protein 2), ROC2 (Regulator of Cullins 2), or RNF7 (RING Finger Protein 7), was originally cloned in our laboratory as a redox inducible antioxidant protein and later characterized as the second member of the RBX/ROC RING component of the SCF (SKP1-CUL-F-box Proteins) E3 ubiquitin ligase. by forming a complex with other components of the SCF E3 ligase, SAG promotes ubiquitination and degradation of a number of protein substrates, including c-JUN, DEPTOR, HIF-1α, IκBα, NF1, NOXA, p27, and procaspase-3, thus regulating various signaling pathways and biological processes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOXA1 | up-regulates quantity by expression 
transcriptional regulation
|
CDKN1B |
0.322 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142940 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 16331276 |
We identified a foxa1 binding site within the brca1-responsive element of the p27(kip1) promoter and showed that foxa1 activated the promoter alone and in conjunction with brca1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 | down-regulates quantity by repression
transcriptional regulation
|
CDKN1B |
0.85 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178269 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18423396 |
Moreover, expression of p27(kip1), an inhibitor of the cell cycle, was down regulated in an akt1/pkbalpha-specific manner during adipocytedifferentiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CUL1 | down-regulates quantity by destabilization
ubiquitination
|
CDKN1B |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102725 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 12835716 |
Furthermore, c-myc activation can also promote the degradation of p27kip1 protein by directly activating the cul1 gene, which encodes a critical component of the ubiquitin ligase scfskp2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDKN1B | down-regulates
binding
|
CDK1 |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128445 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15340381 |
P21 and p27 are key inhibitors of both cdk1 and cdk2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, IDH-TET in AML |
| + |
LRRC4 | up-regulates quantity by expression
transcriptional regulation
|
CDKN1B |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264054 |
|
|
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 |
| + |
CDKN1B | down-regulates
|
Cell_cycle_progress |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241967 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8033212 |
p27Kip1, a cyclin-dependent kinase inhibitor implicated in G1 phase arrest by TGF beta and cell-cell contact. p27Kip1 associates with cyclin E-Cdk2 complexes in vivo and in vitro, prevents their activation, and inhibits previously activated complexes, and p27Kip1 overexpression obstructs cell entry into S phase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDKN1B | up-regulates
|
Cell_cycle_block |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178278 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18423396 |
Moreover, expression of p27(kip1), an inhibitor of the cell cycle, was down regulated in an akt1/pkbalpha-specific manner during adipocytedifferentiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition |
| + |
FOXO3 | up-regulates quantity
transcriptional regulation
|
CDKN1B |
0.746 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-238610 |
|
|
Mus musculus |
NIH-3T3-A14 Cell |
| pmid |
sentence |
| 10783894 |
AFX transcriptionally activates p27kip1, resulting in increased protein levels. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Integrin Signaling |
| + |
AKT | down-regulates
binding
|
CDKN1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200875 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23400686 |
Furthermore, akt promotes cell cycle progression through downregulation of the cyclin dependent kinase inhibitor p27kip1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Integrin Signaling |
| + |
CDKN1B | down-regulates activity
binding
|
CyclinE/CDK2 |
0.882 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217505 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17409098 |
P27, an important cell cycle regulator, blocks the g(1)/s transition in cells by binding and inhibiting cdk2/cyclin a and cdk2/cyclin e complexes (cdk2/e). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G1/S phase transition, Cell cycle: G2/M phase transition, Integrin Signaling |
| + |
TGFB1 | up-regulates quantity by expression
|
CDKN1B |
0.29 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152945 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17283133 |
In normal primary endometrial epithelial cells (eecs), tgfbeta directly induced a dose-dependent increase in p27 protein levels and its nuclear localization |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G1/S phase transition |
| + |
SKP2 | down-regulates
ubiquitination
|
CDKN1B |
0.766 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138493 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15998794 |
Up-regulation of skp2 by notch signaling enhances proteasome-mediated degradation of the ckis, p27 kip1 and p21 cip1, and causes premature entry into s phase. ;the recognition of p27 by skp2/cks1 of the scfskp2 complex is dictated by cycline/cdk2, providing a high affinity binding site and the phosphorylation of p27 at t187, serving here we provide evidence suggesting that both cdk2/e and phosphorylation of thr(187) on p27 are essential for the recognition of p27 by the scf(skp2/cks1) complex, the ubiquitin-protein isopeptide ligase (e3). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154194 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17409098 |
Up-regulation of skp2 by notch signaling enhances proteasome-mediated degradation of the ckis, p27 kip1 and p21 cip1, and causes premature entry into s phase. ;the recognition of p27 by skp2/cks1 of the scfskp2 complex is dictated by cycline/cdk2, providing a high affinity binding site and the phosphorylation of p27 at t187, serving here we provide evidence suggesting that both cdk2/e and phosphorylation of thr(187) on p27 are essential for the recognition of p27 by the scf(skp2/cks1) complex, the ubiquitin-protein isopeptide ligase (e3). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SCF-betaTRCP | down-regulates
ubiquitination
|
CDKN1B |
0.529 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217172 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 12835716 |
Furthermore, c-myc activation can also promote the degradation of p27kip1 protein by directly activating the cul1 gene, which encodes a critical component of the ubiquitin ligase scfskp2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YWHAE | down-regulates
binding
|
CDKN1B |
0.538 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88297 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12042314 |
14-3-3_, 14-3-3_, and 14-3-3_ (but not 14-3-3_ and 14-3-3_) could form a complex with p27kip1 / we discovered that akt-mediated p27kip1phosphorylation directly induces p27kip1binding to 14-3-3 and cytoplasmic localization through phosphorylating the newly identified thr198residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYVN1 | down-regulates quantity by destabilization
ubiquitination
|
CDKN1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278786 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27417417 |
The E3 ligase activity of Hrd1 is required for p27 kip1 ubiquitination, because co-expression of Hrd1 containing an alanine point mutation at the critical cysteine within the RING E3 ligase region (Hrd1/CA) failed to enhance p27 kip1 ubiquitination (XREF_FIG).|Therefore, our study identifies Hrd1 as an E3 ligase of p27 kip1 and establishes that Hrd1 mediated p27 kip1 degradation plays an important role in T-cell immunity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IMPDH2 | down-regulates quantity by repression
transcriptional regulation
|
CDKN1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260960 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30518405 |
We further demonstrated that IMPDH2 overexpression accelerated G1/S phase cell cycle transition by inducing increased expression of cyclin D1 and Ki-67 and downregulation of p21Cip1 and p27Kip1. More importantly, G1/S phase cell cycle transition was triggered by IMPDH2 through activation of AKT activity, downregulation of mTOR and FOXO1 transcriptional activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YWHAQ | down-regulates
binding
|
CDKN1B |
0.522 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88300 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12042314 |
14-3-3_, 14-3-3_, and 14-3-3_ (but not 14-3-3_ and 14-3-3_) could form a complex with p27kip1 / we discovered that akt-mediated p27kip1phosphorylation directly induces p27kip1binding to 14-3-3 and cytoplasmic localization through phosphorylating the newly identified thr198residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KPC | down-regulates quantity by destabilization
polyubiquitination
|
CDKN1B |
0.441 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271513 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15531880 |
We now describe a previously unidentified E3 complex: KPC (Kip1 ubiquitination-promoting complex), consisting of KPC1 and KPC2. KPC1 contains a RING-finger domain, and KPC2 contains a ubiquitin-like domain and two ubiquitin-associated domains. KPC interacts with and ubiquitinates p27(Kip1) and is localized to the cytoplasm. Overexpression of KPC promoted the degradation of p27(Kip1), whereas a dominant-negative mutant of KPC1 delayed p27(Kip1) degradation. Polyubiquitination activity of KPC was apparent with only Ubc4 or UbcH5A. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BRCA1 | up-regulates quantity by expression
transcriptional regulation
|
CDKN1B |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142888 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 16331276 |
We identified a foxa1 binding site within the brca1-responsive element of the p27(kip1) promoter and showed that foxa1 activated the promoter alone and in conjunction with brca1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
CDKN1B | down-regulates
|
Proliferation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261687 |
|
|
Homo sapiens |
SGC-7901 Cell |
| pmid |
sentence |
| 22343731 |
The results of the MTT assay and growth curves revealed that the cells transfected with pEGFP-p27kip1 had a significant growth inhibition when compared with cells transfected with pEGFP-NC (Fig. 5B and D). These data indicated that overexpression of p27kip1 could arrest cell-cycle progression and decrease proliferation of SGC-7901 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, IDH-TET in AML, Integrin Signaling |
| + |
RANBP2 | down-regulates quantity
relocalization
|
CDKN1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259115 |
|
|
Homo sapiens |
Cholangiocarcinoma Cell Line |
| pmid |
sentence |
| 28882106 |
RanBP2 can increase the sumoylation of p27kip1. In our study, the target protein p27kip1 mainly acts as a tumor-suppressor gene in the nucleus, RanBP2 and SUMO1 act as oncogenes by promoting the nuclear-cytoplasmic translocation and debilitate the G1-arrest brought by p27kip1 accumulation in the nucleus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOXO3 | down-regulates quantity by repression
transcriptional regulation
|
CDKN1B |
0.746 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261527 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 14981546 |
Induction of Foxo3a phosphorylation by FLT3-ITD receptors in Ba/F3 cells correlates with the suppression of Foxo-target genes p27Kip1 and the proapoptotic Bcl-2 family member Bim |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Integrin Signaling |
| + |
Gbeta | down-regulates
phosphorylation
|
CDKN1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270087 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10931950 |
These data suggest that increased signaling by erbb receptors up-regulates mapk activity, which, in turn, phosphorylates and destabilizes p27, thus contributing to dysregulated cell cycle progression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FLT3 | down-regulates quantity by repression
transcriptional regulation
|
CDKN1B |
0.29 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261524 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 14981546 |
FLT3-ITD signaling contributes to transcriptional inhibition of p27Kip1 and Bim gene expression |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia |
| + |
YWHAH | down-regulates
binding
|
CDKN1B |
0.499 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109771 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12042314 |
14-3-3_, 14-3-3_, and 14-3-3_ (but not 14-3-3_ and 14-3-3_) could form a complex with p27kip1 / we discovered that akt-mediated p27kip1phosphorylation directly induces p27kip1binding to 14-3-3 and cytoplasmic localization through phosphorylating the newly identified thr198residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MEN1 | up-regulates quantity by expression
transcriptional regulation
|
CDKN1B |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255889 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15640349 |
Menin activates transcription by means of a mechanism involving recruitment of MLL to the p27Kip1 and p18Ink4c promoters and coding regions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
FOXO1 | up-regulates quantity by expression
transcriptional regulation
|
CDKN1B |
0.625 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277739 |
|
|
Homo sapiens |
PANC-1 Cell |
| pmid |
sentence |
| 30519351 |
To date , we have found that TNC regulates the transcriptional activity of FOXO1. And p27Kip1 is one of the transcriptional targets of FOXO1 (Fig. 5A). We speculated that TNC could regulate the binding of FOXO1 to the CDKN1B promoter. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDKN1B
- 
- 