| + |
SCF-SKP2 | down-regulates quantity by destabilization 
polyubiquitination
|
CDK9 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272666 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11689688 |
Here we report that CDK9 is ubiquitinated and degraded by the proteasome whereas cyclin T1 is stable. SCF(SKP2) was recruited to CDK9/cyclin T1 via cyclin T1 in an interaction requiring its PEST domain. CDK9 ubiquitination was modulated by cyclin T1 and p45(SKP2). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-SKP2 | down-regulates quantity by destabilization
ubiquitination, polyubiquitination
|
CDKN1B |
0.697 |
| 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. |
|
| 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. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, In Vitro |
| + |
SKP2 | form complex 
binding
|
SCF-SKP2 |
0.927 |
| 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 |
| + |
SCF-SKP2 | down-regulates quantity by destabilization
ubiquitination
|
CDKN1A |
0.682 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267556 |
|
|
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 9736735 |
Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21CIP1/WAF1 and cyclin D proteins|These data suggest that the human p19(SKP1)/p45(SKP2)/CUL-1 complex is likely to function as an E3 ligase to selectively target cyclin D and p21 for the ubiquitin-dependent protein degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP1 | form complex
binding
|
SCF-SKP2 |
0.941 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243554 |
|
|
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 |
| + |
SCF-SKP2 | down-regulates quantity by destabilization
ubiquitination
|
IDH1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267623 |
|
|
|
|
| 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 |
| + |
SCF-SKP2 | down-regulates quantity by destabilization
ubiquitination
|
CCNE2 |
0.578 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267559 |
|
|
in vitro |
|
| pmid |
sentence |
| 11533444 |
The amount of cyclin E protein present in the cell is tightly controlled by ubiquitin-mediated proteolysis. Here we identify the ubiquitin ligase responsible for cyclin E ubiquitination as SCFFbw7 and demonstrate that it is functionally conserved in yeast, flies, and mammals. Fbw7 associates specifically with phosphorylated cyclin E, and SCFFbw7 catalyzes cyclin E ubiquitination in vitro |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CDC34 | up-regulates activity 
binding
|
SCF-SKP2 |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277334 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25425648 |
The ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase SCF are capable of building polyubiquitin chains onto protein substrates both rapidly and processively; this may be explained at least in part by the atypically fast rate of Cdc34 and SCF association.Here, we use protein cross-linking to demonstrate that the Cdc34-SCF interaction occurs in multiple conformations, where several residues from the Cdc34 acidic tail are capable of contacting a broad region of the SCF basic canyon. Similar patterns of cross-linking are also observed between Cdc34 and the Cul1 paralog Cul2, implicating the same mechanism for the Cdc34-SCF interaction in other members of the cullin-RING ubiquitin ligases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-SKP2 | down-regulates quantity by destabilization
ubiquitination
|
MEF2D |
0.288 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276889 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 25733682 |
MEF2C and MEF2D interact with the E3 ligase F-box protein SKP2, which mediates their subsequent degradation through the ubiquitin-proteasome system. The cyclin-dependent kinase 4 (CDK4)/cyclin D1 complex phosphorylates MEF2D on serine residues 98 and 110, and phosphorylation of these residues is an important determinant for SKP2 binding. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SCF-SKP2 | down-regulates quantity by destabilization
polyubiquitination
|
RBL2 |
0.565 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272598 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12435635 |
The activity of the ubiquitin ligase complex Skp1-Cul1/Cdc53-F-box protein Skp2 (SCF(Skp2)) and the proteasome were necessary for p130 degradation. In vitro, recombinant Skp2 was able to bind hyperphosphorylated but not dephosphorylated p130. Furthermore, in vitro polyubiquitination of p130 by SCF(Skp2) was specifically dependent on phosphorylation of p130 on Serine 672. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-SKP2 | down-regulates quantity by destabilization
ubiquitination
|
CCNE1 |
0.649 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267558 |
|
|
in vitro |
|
| pmid |
sentence |
| 11533444 |
The amount of cyclin E protein present in the cell is tightly controlled by ubiquitin-mediated proteolysis. Here we identify the ubiquitin ligase responsible for cyclin E ubiquitination as SCFFbw7 and demonstrate that it is functionally conserved in yeast, flies, and mammals. Fbw7 associates specifically with phosphorylated cyclin E, and SCFFbw7 catalyzes cyclin E ubiquitination in vitro |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SCF-SKP2 | down-regulates quantity
ubiquitination
|
MYC |
0.568 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243551 |
|
|
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 |
| + |
SCF-SKP2 | down-regulates quantity by destabilization
polyubiquitination
|
E2F1 |
0.381 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272557 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 10559858 |
P45 SKP2 binds to a specific domain of E2F-1. We propose a model in which an SCFSKP2-dependent ubiquitination pathway contributes to the timely ubiquitination and degradation of E2F-1 in the S/G2 phases of the cell cycle. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CUL1 | form complex
binding
|
SCF-SKP2 |
0.945 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243557 |
|
|
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 |
4.0
SCF-SKP2