+ |
SRC | up-regulates
phosphorylation
|
CBLC |
0.551 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165862 |
Tyr341 |
SEEQLQLyWAMDSTF |
Homo sapiens |
|
pmid |
sentence |
20525694 |
Phosphorylation of a critical tyrosine (tyr-341) in the linker region of cbl-c by src or a phosphomimetic mutation of this tyrosine (y341e) is sufficient to increase the e3 activity of cbl-c. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SPRY2 | down-regulates
|
CBLC |
0.46 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-92926 |
|
|
Homo sapiens |
|
pmid |
sentence |
12234920 |
Hspry2 prevents c-cbl-mediated ubiquitylation of egfrs. hspry2 interacts specifically with the c-cbl ring finger domain and displaces ubch7 from its binding site on the e3 ligase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBLC | down-regulates
ubiquitination
|
LRIG1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-127292 |
|
|
Homo sapiens |
|
pmid |
sentence |
15282549 |
Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Skin |
+ |
INPPL1 | down-regulates
binding
|
CBLC |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-133388 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
15668240 |
This association between ship2 and cbl could sequester cbl from the egfr, thereby regulating the kinetics of egfr-cbl association and subsequent internalization and degradation of the receptor. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LRIG1 | up-regulates
binding
|
CBLC |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-127301 |
|
|
Homo sapiens |
|
pmid |
sentence |
15282549 |
Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Skin |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
CBLC |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271060 |
|
|
Homo sapiens |
|
pmid |
sentence |
34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EPHB6 | up-regulates activity
binding
|
CBLC |
0.276 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273852 |
|
|
Homo sapiens |
|
pmid |
sentence |
34360976 |
We suggest that although mammalian EphB6 is kinase-negative, it has retained the allosteric regulatory mechanisms involving the juxtamembrane and the SAM domain linker that are used to regulate the kinase activity of kinase-active Eph receptors. he inability to recruit c-Cbl by EphB6 meant that heightened levels of EphA2 remained active in the cell because they had evaded c-Cbl-mediated degradation. The authors suggest that mutation of residues 901–926 within EphB6 reduces the flexibility of the SAM domain such that c-Cbl cannot be recruited. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ARHGEF7 | down-regulates
binding
|
CBLC |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118135 |
|
|
Homo sapiens |
|
pmid |
sentence |
14505571 |
Here, we show that activation of cdc42 protects the egf receptor from the negative regulatory activity of the c-cbl ubiquitin ligase. Activated cdc42 binds to p85cool-1 (for cloned-out-of-library)/beta-pix (for pak-interactive exchange factor), a protein that directly associates with c-cbl. This inhibits the binding of cbl by the egf receptor and thus prevents cbl from catalyzing receptor ubiquitination |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBLC | down-regulates quantity by destabilization
polyubiquitination
|
EGFR |
0.762 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272605 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
12226085 |
In summary, we have shown that CBLC and AIP4 can interact and that these two E3 ligases could contribute to down-regulate EGFR signaling by ubiquitination. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |