| + |
PIM1 | up-regulates activity 
phosphorylation
|
SKP2 |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259818 |
Ser64 |
SNLGHPEsPPRKRLK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 20663873 |
We found that expression of Pim-1 increases the level of Skp2 through direct binding and phosphorylation of multiple sites on this protein. Along with known Skp2 phosphorylation sites including Ser(64) and Ser(72), we have identified Thr(417) as a unique Pim-1 phosphorylation target. Phosphorylation of Thr(417) controls the stability of Skp2 and its ability to degrade p27. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259819 |
Ser72 |
PPRKRLKsKGSDKDF |
Homo sapiens |
|
| pmid |
sentence |
| 20663873 |
We found that expression of Pim-1 increases the level of Skp2 through direct binding and phosphorylation of multiple sites on this protein. Along with known Skp2 phosphorylation sites including Ser(64) and Ser(72), we have identified Thr(417) as a unique Pim-1 phosphorylation target. Phosphorylation of Thr(417) controls the stability of Skp2 and its ability to degrade p27. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259817 |
Thr417 |
WGIKCRLtLQKPSCL |
Homo sapiens |
|
| pmid |
sentence |
| 20663873 |
We found that expression of Pim-1 increases the level of Skp2 through direct binding and phosphorylation of multiple sites on this protein. Along with known Skp2 phosphorylation sites including Ser(64) and Ser(72), we have identified Thr(417) as a unique Pim-1 phosphorylation target. Phosphorylation of Thr(417) controls the stability of Skp2 and its ability to degrade p27. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK2 | up-regulates quantity by stabilization
phosphorylation
|
SKP2 |
0.792 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249173 |
Ser64 |
SNLGHPEsPPRKRLK |
|
|
| pmid |
sentence |
| 18239684 |
The activity of SCF(Skp2) is regulated by the Cyclin-dependent kinase (CDK)2-mediated phosphorylation of Skp2 on Ser64 allows its expression in mid-G1 phase, even in the presence of active APC(Cdh1). Reciprocally, dephosphorylation of Skp2 by the mitotic phosphatase Cdc14B at the M --> G1 transition promotes its degradation by APC(Cdh1). |
|
| Publications: |
1 |
| + |
CDC14B | down-regulates quantity by destabilization 
dephosphorylation
|
SKP2 |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248333 |
Ser64 |
SNLGHPEsPPRKRLK |
Homo sapiens |
|
| pmid |
sentence |
| 18239684 |
The activity of SCF(Skp2) is regulated by the Cyclin-dependent kinase (CDK)2-mediated phosphorylation of Skp2 on Ser64 allows its expression in mid-G1 phase, even in the presence of active APC(Cdh1). Reciprocally, dephosphorylation of Skp2 by the mitotic phosphatase Cdc14B at the M --> G1 transition promotes its degradation by APC(Cdh1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP2 | down-regulates quantity by destabilization
binding
|
NUDT1 |
0.256 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272790 |
|
|
Homo sapiens |
Mel-CV Cell |
| pmid |
sentence |
| 28947420 |
Here, we report that MTH1 is regulated by polyubiquitination mediated by the E3 ligase Skp2. In melanoma cells, MTH1 was upregulated commonly mainly due to its improved stability caused by K63-linked polyubiquitination. Although Skp2 along with other components of the Skp1-Cullin-F-box (SCF) ubiquitin ligase complex was physically associated with MTH1, blocking the SCF function ablated MTH1 ubiquitination and expression. Conversely, overexpressing Skp2-elevated levels of MTH1 associated with an increase in its K63-linked ubiquitination. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
SKP2 |
0.918 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272574 |
|
|
in vitro |
|
| pmid |
sentence |
| 11032804 |
These results suggest that degradation of Skp2 in G(0)/G(1) is mediated, at least in part, by an autocatalytic mechanism involving a Skp2-bound Cul1-based core ubiquitin ligase and imply a role for this mechanism in the suppression of SCF(Skp2) ubiquitin protein ligase function during the G(0)/G(1) phases of the cell cycle. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SKP2 | down-regulates quantity
ubiquitination
|
MYC |
0.726 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243548 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20852628 |
The F-box protein Skp2 mediates c-Myc ubiquitylation by binding to the MB2 domain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TGFB1 | down-regulates 
|
SKP2 |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171013 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21212736 |
Skp2, a f-box protein that determines the substrate specificity for scf ubiquitin ligase, has recently been demonstrated to be degraded by cdh1/apc in response to tgfbeta signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP2 | down-regulates quantity by destabilization
binding
|
CDT1 |
0.68 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272565 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10790373 |
Biochemical studies showed that Skp2 interacts specifically with cyclin E and thereby promotes its ubiquitylation and degradation both in vivo and in vitro. These results suggest that specific degradation of cyclin E and p27(Kip1) is mediated by the SCF(Skp2) ubiquitin ligase complex, and that Skp2 may control chromosome replication and centrosome duplication by determining the abundance of cell cycle regulators. Skp2 was associated with Cul1, but not Cul3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP2 | up-regulates activity
binding
|
Cullin 1-RBX1-Skp1 |
0.918 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272576 |
|
|
Homo sapiens |
SK-UT-1B Cell |
| pmid |
sentence |
| 11439327 |
We show that SK-UT-1B cells express a novel splice variant of Skp2 that localizes to the cytoplasm and that cyclin D1 ubiquitination takes place in the nucleus. We propose that the translocation of Skp2 into the nucleus is required for the ubiquitination of cyclin D1 and that the absence of the SCF(Skp2) complex in the nucleus of SK-UT-1B cells is the mechanism underlying the ubiquitination defect observed in this cell line. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272567 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10790373 |
Biochemical studies showed that Skp2 interacts specifically with cyclin E and thereby promotes its ubiquitylation and degradation both in vivo and in vitro. These results suggest that specific degradation of cyclin E and p27(Kip1) is mediated by the SCF(Skp2) ubiquitin ligase complex, and that Skp2 may control chromosome replication and centrosome duplication by determining the abundance of cell cycle regulators. Skp2 was associated with Cul1, but not Cul3. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SKP2 | up-regulates
binding
|
Cullin 1-RBX1-Skp1 |
0.918 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272793 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28948618 |
Skp2 induces ubiquitin-dependent degradation of Cygb. To this end, we performed an in vivo ubiquitination assay in HEK293T cells by transfecting relevant plasmids as indicated. The V5-Skp2DN was generated by deleting the N-terminal residues from 1 to 153 containing the F-box domain, which is involved in recruiting Skp2 to the SCF complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP2 | down-regulates quantity by destabilization
binding
|
CCNE1 |
0.694 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272566 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10790373 |
Biochemical studies showed that Skp2 interacts specifically with cyclin E and thereby promotes its ubiquitylation and degradation both in vivo and in vitro. These results suggest that specific degradation of cyclin E and p27(Kip1) is mediated by the SCF(Skp2) ubiquitin ligase complex, and that Skp2 may control chromosome replication and centrosome duplication by determining the abundance of cell cycle regulators. Skp2 was associated with Cul1, but not Cul3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP2 | down-regulates quantity by destabilization
ubiquitination
|
IDH1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267625 |
|
|
|
|
| pmid |
sentence |
| 34929314 |
During the cell cycle S phase, Cyclin A-CDK2 phosphorylates IDH1 on its Threonine 157 residue (Threonine 197 in IDH2) to facilitate its recognition and ubiquitination by Skp2 E3 ubiquitin, followed by degradation through 26S proteasome |
|
| Publications: |
1 |
| + |
SKP2 | down-regulates quantity by destabilization
ubiquitination
|
IDH2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267626 |
|
|
|
|
| pmid |
sentence |
| 34929314 |
During the cell cycle S phase, Cyclin A-CDK2 phosphorylates IDH1 on its Threonine 157 residue (Threonine 197 in IDH2) to facilitate its recognition and ubiquitination by Skp2 E3 ubiquitin, followed by degradation through 26S proteasome |
|
| Publications: |
1 |
| + |
SKP2 | down-regulates
ubiquitination
|
SMAD4 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-127964 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15314162 |
We found that skp2, the f-box component of scfskp2, physically interacted with smad4 at the physiological levels. Several cancer-derived unstable mutants exhibited significantly increased binding to skp2, which led to their increased ubiquitination and accelerated proteolysis. These results suggest an important role for the scfskp2 complex in switching cancer mutants of smad4 to undergo polyubiquitination-dependent degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP2 | down-regulates
ubiquitination
|
CDKN1A |
0.763 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138490 |
|
|
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. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP2 | down-regulates quantity by destabilization
ubiquitination
|
DAB2IP |
0.271 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254775 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27858941 |
DAB2IP protein levels can be negatively regulated by the activity of the E3-ubiquitin ligases Fbw7, Skp2, and Smurf1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP2 | down-regulates quantity by destabilization
binding
|
CCND1 |
0.577 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272575 |
|
|
Homo sapiens |
SK-UT-1B Cell |
| pmid |
sentence |
| 11439327 |
We show that SK-UT-1B cells express a novel splice variant of Skp2 that localizes to the cytoplasm and that cyclin D1 ubiquitination takes place in the nucleus. We propose that the translocation of Skp2 into the nucleus is required for the ubiquitination of cyclin D1 and that the absence of the SCF(Skp2) complex in the nucleus of SK-UT-1B cells is the mechanism underlying the ubiquitination defect observed in this cell line. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP2 | down-regulates quantity by destabilization
polyubiquitination
|
MYBL2 |
0.386 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272572 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10871850 |
P19Skp1 and Cul-1 bind to the F-box protein p45Skp2 to form a complex (SCF) that functions as E3 ubiquitin ligase.We show that B-Myb physically and functionally interacts with components of the Cdc34-SCFp45Skp2 ubiquitin pathway and propose that B-Myb degradation may be required for controlling the correct alternation of events during progression through the cell division cycle. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP2 | down-regulates
ubiquitination
|
CDKN1B |
0.757 |
| 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 |
| + |
SKP2 | form complex 
binding
|
SCF-SKP2 |
0.925 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243560 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15340381 |
The F-box family of proteins which are the substrate-recognition components of the Skp1Cul1F-box-protein (SCF) ubiquitin ligase are important players in many mammalian functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP2 | down-regulates quantity by destabilization
binding
|
CYGB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272792 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28948618 |
Skp2 induces ubiquitin-dependent degradation of Cygb. To this end, we performed an in vivo ubiquitination assay in HEK293T cells by transfecting relevant plasmids as indicated. The V5-Skp2DN was generated by deleting the N-terminal residues from 1 to 153 containing the F-box domain, which is involved in recruiting Skp2 to the SCF complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SKP2
- 
- 