+ |
CBLB | down-regulates quantity
ubiquitination
|
STAT6 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278805 |
Lys108 |
QILQGEKkAVMEQFR |
Homo sapiens |
|
pmid |
sentence |
24508458 |
Having shown that Cbl-b negatively regulates Stat6, we further investigated the mechanism of this regulation by determining whether Cbl-b associates with Stat6.|Our data demonstrate that Stat6 is ubiquitinated at K108 and K398 by Cbl-b, and that Stat6 ubiquitination is a critical post-translational regulatory mechanism for Stat6. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278806 |
Lys398 |
SFTLGPGkLPIQLQA |
Homo sapiens |
|
pmid |
sentence |
24508458 |
Having shown that Cbl-b negatively regulates Stat6, we further investigated the mechanism of this regulation by determining whether Cbl-b associates with Stat6.|Our data demonstrate that Stat6 is ubiquitinated at K108 and K398 by Cbl-b, and that Stat6 ubiquitination is a critical post-translational regulatory mechanism for Stat6. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CBLB | down-regulates quantity
ubiquitination
|
NTRK1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278690 |
|
|
Homo sapiens |
|
pmid |
sentence |
35288194 |
Cbl-b modulated TrkA ubiquitination and function in the dorsal root ganglion of mice.|Viral expression of constitutively active Cbl-b in DRGs of osteoarthritic mice effectively repressed TrkA protein level and more importantly, alleviated mechanical allodynia and heat hyperalgesia. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBLB | down-regulates quantity
ubiquitination
|
SYK |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278754 |
|
|
Homo sapiens |
|
pmid |
sentence |
12771181 |
In summary, the studies presented here provide evidence that Cbl-b negatively regulates Syk through ubiquitination.|The results presented suggest that Cbl-b ubiquitinates active phosphorylated Syk and thus functions to dampen B cell antigen receptor signaling after signaling is initiated and thus plays a role in the normal down modulation of B cell antigen receptor signaling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBLB | up-regulates activity
ubiquitination
|
TYRO3 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278807 |
|
|
Homo sapiens |
|
pmid |
sentence |
31531847 |
Consistent with these data, we also found that Tyro3 is ubiquitinated by Cbl-b.|These data suggest that not only was Tyro3 a ubiquitination target of Cbl-b, but also that Cbl-b was a phosphorylation target of Tyro3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBLB | up-regulates activity
binding
|
NCK1 |
0.508 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236054 |
|
|
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
16503409 |
Activated Cbl and Cbl-b interacted with Crk-L, Zap-70, Nck, PLC-gamma |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | EGFR Signaling |
+ |
CBLB | up-regulates activity
|
TP53 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261320 |
|
|
Homo sapiens |
MOLM-13 Cell |
pmid |
sentence |
27773928 |
We have also shown that the E3 ubiquitin ligase Cbl-b is crucial for activation of the p53 pathway through ubiquitinating and promoting degradation of Siva1, the E3 ubiquitin ligase targeting ARF, a positive regulator of p53. On the basis of our data presented in the study, we propose the model (Figure 2i) that Cbl-b negatively regulates Siva1 by ubiquitination and subsequent degradation of Siva1, which is followed by stabilization of ARF. This in turn downregulates MDM2, thereby promoting the induction of p53 and activation of its downstream targets. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, KIT in AML |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
CBLB |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271055 |
|
|
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 |
+ |
SPRY2 | down-regulates
binding
|
CBLB |
0.495 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83507 |
|
|
Homo sapiens |
|
pmid |
sentence |
11053437 |
One function of hspry2 in signaling processes downstream of rtks may be to modulate c-cbl physiological function such as that seen with receptor-mediated endocytosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBLB | down-regulates quantity by destabilization
polyubiquitination
|
PIK3R1 |
0.499 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272583 |
|
|
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
11087752 |
Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells.Here it is shown that Cbl-b interacts with and induces ubiquitin conjugation to the p85 regulatory subunit of phosphatidylinositol 3-kinase, an upstream regulator of Vav. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBLB | down-regulates activity
ubiquitination
|
KIT |
0.331 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260105 |
|
|
Homo sapiens |
|
pmid |
sentence |
15315962 |
KIT binds to and induces the phosphorylation of Cbl proteins, which in turn act as E3 ligases, mediating the ubiquitination and degradation of KIT and themselves. Tyrosine kinase binding and RING finger domains of Cbl are essential for Cbl-mediated ubiquitination and degradation of KIT. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, KIT in AML |
+ |
CBLB | down-regulates activity
ubiquitination
|
EGFR |
0.75 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236519 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11375397 |
Cbl proteins function as ubiquitin protein ligases for the activated epidermal growth factor receptor and, thus, negatively regulate its activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, EGFR Signaling |
+ |
CBLB | down-regulates activity
ubiquitination
|
PIK3R2 |
0.484 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271424 |
|
|
Homo sapiens |
JURKAT Cell |
pmid |
sentence |
11087752 |
Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells. it can be postulated that Cbl-b, as an E3 Ub ligase, may play a general role in functional regulation of its target proteins through ubiquitination in a protein degradation-independent manner. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBLB | down-regulates quantity by destabilization
polyubiquitination
|
EGFR |
0.75 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272934 |
|
|
Homo sapiens |
|
pmid |
sentence |
10542134 |
Here we describe that overexpression of cbl-b, a homologue of the c-cbl protooncogene, inhibits EGFR-induced apoptosis in MDA-MB-468 breast cancer cells. Overexpression of cbl-b results in a shortened duration of EGFR activation upon EGF stimulation. This is demonstrated by decreased amounts of phosphorylated EGFR as well as by inhibition of multiple downstream signaling pathways. The inhibition of signaling by cbl-b results from increased ubiquitination and degradation of the activated EGFR. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, EGFR Signaling |
+ |
CBLB | down-regulates activity
ubiquitination
|
FLT3 |
0.33 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260106 |
|
|
Mus musculus |
BA/F3 Cell |
pmid |
sentence |
19276253 |
Functionally, CBL negatively regulated FMS-like tyrosine kinase 3 (FLT3) activity and interacted with human FLT3 via the autophosphorylation sites Y589 and Y599 and colocalized in vivo. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Pathways: | Acute Myeloid Leukemia, FLT3 in AML |
+ |
CBLB | down-regulates quantity by destabilization
ubiquitination
|
IGF1R |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278607 |
|
|
Homo sapiens |
|
pmid |
sentence |
24885194 |
The ubiquitin ligase Cbl-b also ubiquitinated and degraded IGF-IR and inhibited the Akt/ERK-miR-200c-ZEB2 axis, leading to the repression of IGF-I-induced EMT. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBLB | up-regulates activity
binding
|
GRB2 |
0.58 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236051 |
|
|
Homo sapiens |
JURKAT Cell |
pmid |
sentence |
8626404 |
Here we show that in unstimulated Jurkat cells Cbl is co-immunoprecipitated with monoclonal antibody against Grb2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, EGFR Signaling |
+ |
CBLB | down-regulates quantity by destabilization
ubiquitination
|
CLEC6A |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278625 |
|
|
Homo sapiens |
|
pmid |
sentence |
27432944 |
Furthermore, we found that Cbl-b, an E3 ubiquitin ligase, mediates the ubiquitination and degradation of the activated Dectin-2 and Dectin-3 to negatively regulate CLR mediated innate immune responses against fungal infections. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |