+ |
SKP1 | form complex
binding
|
SCF-FBW2 |
0.842 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271526 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
15640526 |
FBW2 targets GCMa to the ubiquitin-proteasome degradation system. Here, we report the identification of an SCF complex as the GCM ubiquitin-protein isopeptide ligase (E3) that regulates human GCMa (hGCMa) degradation. We found that SKP1 and CUL1, two key components of the SCF complex, associate with hGCMa in vivo. We further identify the human F-box protein FBW2 (hFBW2) as the substrate recognition subunit in the SCF E3 complex for hGCMa. We show that hFBW2 interacts with hGCMa in a phosphorylation-dependent manner and promotes hGCMa ubiquitination. Supporting a critical role for hFBW2 in hGCMa degradation, knockdown of hFBW2 expression by RNA interference leads to a reduction in hGCMa ubiquitination and a concomitant increase in hGCMa protein stability. Our study identifies the SCF(hFBW2) E3 complex as the key machinery that targets hGCMa to the ubiquitin-proteasome degradation system |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SKP1 | form complex
binding
|
Skp1-Pam E3 |
0.427 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272185 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
25460509 |
One of the hallmarks of EMT is loss of E-cadherin and gain of N-cadherin expression, which are regulated by the core EMT-inducing transcription factors (EMT-TFs), such as Zeb1/2, Snai1/2 and Twist1. Here, we find that EMT-TFs can be dynamically degraded by an atypical ubiquitin E3 ligase complex Skp1-Pam-Fbxo45 (SPFFbxo45) through the ubiquitin proteasome system (UPS). The key step is recognition of EMT-TFs by Fbxo45 through its SPRY domain for Zeb2, or F-box domain for the other three EMT-TFs Snai1, Snai2 and Twist1, respectively. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SKP1 | up-regulates
binding
|
CUL1 |
0.958 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-64511 |
|
|
Homo sapiens |
|
pmid |
sentence |
10023660 |
The human f box protein beta-trcp associates with the cul1/skp1 complex and regulates the stability of beta-catenin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXW11 | up-regulates
binding
|
SKP1 |
0.793 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-64505 |
|
|
Homo sapiens |
|
pmid |
sentence |
10023660 |
The scf is composed of skp1, cdc53/cul1, and a specificity-conferring f-box protein. F-box proteins contain two domains, an f-box motif that binds skp1 and allows assembly into skp1/cdc53 complexes, and a second proteinprotein interaction domain that interacts specifically with one or more target proteins. Cdc53/cul1, in turn, interacts with both the e2 and the skp1/f-box protein complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SKP1 | form complex
binding
|
SCF-SKP2 |
0.94 |
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 |
+ |
SKP1 | form complex
binding
|
SCF(TBL1) |
0.5 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271950 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
20181957 |
Upon UV-induced DNA damage, beta-catenin is recruited for polyubiquitination and subsequent proteasomal degradation by a unique, p53-induced SCF-like complex (SCF(TBL1)), comprised of Siah-1, Siah-1-interacting protein (SIP), Skp1, transducin beta-like 1 (TBL1), and adenomatous polyposis coli (APC). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SKP1 | up-regulates activity
binding
|
Cullin 3-RBX1-Skp1 |
0.9 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271619 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16547521 |
KLHL12 recruits Dsh to Cullin-3 for protein degradation. In vitro ubiquitination of Dsh3 by KLHL12–Cullin-3–Roc1. The E3 ligase complex was obtained by transfection of HEK293T cells . We show that the BTB-containing protein KLHL12 negatively regulates Dsh function by recruiting a pool of Dsh to the Cullin-3 ligase scaffold, thereby promoting its ubiquitination and degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SKP1 | form complex
binding
|
Cullin 7-RBX1-Skp1 |
0.833 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271627 |
|
|
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
17205132 |
FBXW8 associates with CUL1 or CUL7 and forms a complex with SKP1 and RBX1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SKP1 | form complex
binding
|
SCF-betaTRCP |
0.892 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-64514 |
|
|
Homo sapiens |
|
pmid |
sentence |
10023660 |
The human f box protein beta-trcp associates with the cul1/skp1 complex and regulates the stability of beta-catenin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SKP1 | form complex
binding
|
Cullin 3-RBX1-Skp1 |
0.9 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271620 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16547521 |
KLHL12 recruits Dsh to Cullin-3 for protein degradation. In vitro ubiquitination of Dsh3 by KLHL12–Cullin-3–Roc1. The E3 ligase complex was obtained by transfection of HEK293T cells . We show that the BTB-containing protein KLHL12 negatively regulates Dsh function by recruiting a pool of Dsh to the Cullin-3 ligase scaffold, thereby promoting its ubiquitination and degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SKP1 | form complex
binding
|
Noncanonical PRC1 |
0.452 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255278 |
|
|
Mus musculus |
|
pmid |
sentence |
25533466 |
inhibition of adipogenesis does not require the JmjC demethylase domain of FBXL10, but it does require the F-box and leucine-rich repeat domains, which we show recruit a noncanonical polycomb repressive complex 1 (PRC1) containing RING1B, SKP1, PCGF1, and BCOR. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
SKP1 | form complex
binding
|
SCF-FBW7 |
0.935 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-243760 |
|
|
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 |
+ |
SKP1 | form complex
binding
|
Cullin 1-RBX1-Skp1 |
0.956 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271630 |
|
|
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
17205132 |
FBXW8 associates with CUL1 or CUL7 and forms a complex with SKP1 and RBX1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |