| + |
STUB1 | down-regulates quantity by destabilization 
ubiquitination
|
CBX4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277513 |
Lys178 |
LQYQGGHkEAPSPTC |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 32111827 |
The phosphorylation of CBX4 at T437 by casein kinase 1α (CK1α) facilitated its ubiquitination at both K178 and K280 and subsequent degradation by CHIP, and this phosphorylation of CBX4 could be reduced by TNFα. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277514 |
Lys280 |
GMQAVKIkSGEVAEG |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 32111827 |
The phosphorylation of CBX4 at T437 by casein kinase 1α (CK1α) facilitated its ubiquitination at both K178 and K280 and subsequent degradation by CHIP, and this phosphorylation of CBX4 could be reduced by TNFα. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
BAG1 | up-regulates activity 
binding
|
STUB1 |
0.556 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272587 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 11676916 |
BAG-1 stimulates CHIP-induced degradation of the glucocorticoid hormone receptor (GR). A model for the cooperation of CHIP and BAG-1 in coupling Hsc/Hsp70 to the ubiquitin/proteasome system. CHIP associates with Hsc/Hsp70 via its TPR chaperone adaptor (TPR) and, at the same time, recruits E2 ubiquitin-conjugating enzymes of the Ubc4/5 family to the chaperone complex. BAG-1 binds to Hsp70 via its BAG domain (BAG) and utilizes its ubiquitin-like domain (ubl) for proteasomal association |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
S100P |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272919 |
|
|
in vitro |
|
| pmid |
sentence |
| 23344957 |
S100 protein itself is ubiquitinated by CHIP in a Ca2+-dependent manner.Ubiquitylated S100 proteins are shown as (Ub)n-S100A2 and (Ub)n-S100P. The association of the S100 proteins with CHIP provides a Ca2+-dependent regulatory mechanism for the ubiquitination and degradation of intracellular proteins by the CHIP-proteasome pathway. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STUB1 | up-regulates activity
binding
|
PRKN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272888 |
|
|
in vitro |
|
| pmid |
sentence |
| 12150907 |
In this study, we found that CHIP promotes Parkin-mediated Pael-R ubiquitination and subsequent degradation. In vitro ubiquitination assays suggested that only a combination of both Parkin and its cofactor CHIP function as a ubiquitin ligase, which is able to sufficiently ubiquitinate Pael-R in vivo (Figure 6). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
HSPA8 |
0.731 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272588 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 11676916 |
BAG-1 stimulates CHIP-induced degradation of the glucocorticoid hormone receptor (GR). A model for the cooperation of CHIP and BAG-1 in coupling Hsc/Hsp70 to the ubiquitin/proteasome system. CHIP associates with Hsc/Hsp70 via its TPR chaperone adaptor (TPR) and, at the same time, recruits E2 ubiquitin-conjugating enzymes of the Ubc4/5 family to the chaperone complex. BAG-1 binds to Hsp70 via its BAG domain (BAG) and utilizes its ubiquitin-like domain (ubl) for proteasomal association |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
STUB1 | down-regulates quantity by destabilization
ubiquitination
|
TAL1 |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271393 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 17962192 |
Ubiquitination and degradation of Tal1/SCL are induced by notch signaling and depend on Skp2 and CHIP. CHIP promoted Tal1 degradation with both chaperone binding and ubiquitin ligase activities, which are mediated by its TPR domain and U box, respectively. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
STUB1 | down-regulates quantity by destabilization
destabilization
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274979 |
|
|
Homo sapiens |
A-375 Cell |
| pmid |
sentence |
| 28813410 |
Deletion of STUB1 resulted in a more profound increase in PD-L1 levels in CMTM6 deficient than in CMTM6 proficient cells, identifying STUB1 as an E3 ligase that causes destabilization of PD-L1 (Fig. 4f,g), either by direct modification of one of the lysines in the PD-L1 cytoplasmic domain or indirectly |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
ubiquitination
|
HIF1A |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271426 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19940151 |
the ubiquitin ligase activity of CHIP regulates HIF-1α degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates
ubiquitination
|
SMAD5 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172996 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21454478 |
In addition, some proteins (e.g. Chip, carboxyl terminus of hsc70-interacting protein) inhibit the signaling activities of smad1/5 by recruiting smad1/5 from the functional r/co-smad complex and further promoting the ubiquitination and degradation of smad1/5 in a chaperone-independent manner |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195690 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
In ad-dition, some proteins (e.g. Chip, carboxyl terminus of hsc70-interacting protein) inhibit the signaling activi-ties of smad1/5 by recruiting smad1/5 from the functional r-/co-smad complex and further pro-moting the ubiquitination and degradation of smad1/5 in a chaperone-independent manne |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
CFTR |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272584 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11146634 |
Here we show that CHIP functions with Hsc70 to sense the folded state of CFTR and targets aberrant forms for proteasomal degradation by promoting their ubiquitination. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
S100A2 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272918 |
|
|
in vitro |
|
| pmid |
sentence |
| 23344957 |
S100 protein itself is ubiquitinated by CHIP in a Ca2+-dependent manner.Ubiquitylated S100 proteins are shown as (Ub)n-S100A2 and (Ub)n-S100P. The association of the S100 proteins with CHIP provides a Ca2+-dependent regulatory mechanism for the ubiquitination and degradation of intracellular proteins by the CHIP-proteasome pathway. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STUB1 | down-regulates
ubiquitination
|
SMAD1 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172993 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21454478 |
In ad-dition, some proteins (e.g. Chip, carboxyl terminus of hsc70-interacting protein) inhibit the signaling activities of smad1/5 by recruiting smad1/5 from the functional r-/co-smad complex and further pro-moting the ubiquitination and degradation of smad1/5 in a chaperone-independent manner |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195687 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
In ad-dition, some proteins (e.g. Chip, carboxyl terminus of hsc70-interacting protein) inhibit the signaling activities of smad1/5 by recruiting smad1/5 from the functional r-/co-smad complex and further pro-moting the ubiquitination and degradation of smad1/5 in a chaperone-independent manner |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120731 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14701756 |
These results suggest that chip can interact with the smad1/smad4 proteins and block bmp signal transduction through the ubiquitin-mediated degradation of smad proteins. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
ERBB2 |
0.611 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272586 |
|
|
in vitro |
|
| pmid |
sentence |
| 12239347 |
We now show that the chaperone-binding ubiquitin ligase CHIP efficiently ubiquitinates and down-regulates ErbB2. CHIP expression shortens the half-life of both nascent and mature ErbB2 protein. In vitro ubiquitination assay shows that CHIP serves as a ubiquitin ligase for ErbB2, and both exogenously expressed and endogenous CHIP coprecipitate with the kinase. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
CIP2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272877 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24293411 |
CHIP is the ubiquitin E3 ligase mediating celastrol-triggered CIP2A degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
NRK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274110 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32162334 |
Our results indicate that Nrk is ubiquitinated by CHIP in a chaperone-dependent manner, resulting in its proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXO2 | up-regulates activity
binding
|
STUB1 |
0.573 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271589 |
|
|
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 16682404 |
Through this novel interaction, which is mediated by the TPR domain of CHIP and an N-terminal PEST domain of Fbx2, CHIP facilitates the ubiquitination and degradation of Fbx2-bound glycoproteins. This study highlights a novel mechanism of F-box protein-mediated ubiquitination that contributes to glycoprotein homeostasis. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
SMAD1 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272948 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14701756 |
CHIP mediates the ubiquitination of Smad1. we demonstrate that the coexpression of Smad1 and Smad4 with the CHIP protein results in the degradation of the Smad proteins through a ubiquitin-mediated process. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
PSMD4 |
0.431 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272752 |
|
|
in vitro |
|
| pmid |
sentence |
| 19240029 |
S5a/Rpn10 is a ubiquitin (Ub)-binding protein that is a subunit of the 26S proteasome but also exists free in the cytosol. It binds poly-Ub chains through its two Ub-interacting motifs (UIMs). We discovered that, unlike typical substrates of Ub ligases (E3s), S5a can be ubiquitinated by all E3s tested including multimeric and monomeric Ring finger E3s (MuRF1, Siah2, Parkin, APC, and SCF(betaTRCP1)), the U-box E3, CHIP, and HECT domain E3s (E6AP and Nedd4) when assayed with UbcH5 or related Ub-conjugating enzymes.The short half-life of S5a presumably is because of the presence of the UIM domain and reflects the ubiquitination of free S5a by many E3s. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
ATCAY |
0.386 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272651 |
|
|
in vitro |
|
| pmid |
sentence |
| 16275660 |
CHIP e.g. was found to efficiently polyubiquitinate caytaxin in vitro, suggesting that it might influence caytaxin degradation in vivo. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
SMG5 |
0.408 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272649 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16809764 |
Here, we report that the human ortholog of the yeast ever-shorter telomeres 1B (EST1B) binds HDAC8. This interaction is regulated by protein kinase A-mediated HDAC8 phosphorylation and protects human EST1B (hEST1B) from ubiquitin-mediated degradation. Phosphorylated HDAC8 preferentially recruits Hsp70 to a complex that inhibits the CHIP (C-terminal heat shock protein interacting protein) E3 ligase-mediated degradation of hEST1B. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
SMAD4 |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272947 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14701756 |
We demonstrate that the coexpression of Smad1 and Smad4 with the CHIP protein results in the degradation of the Smad proteins through a ubiquitin-mediated process. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
IRS4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277616 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 30026872 |
IRS4 was phosphorylated at Ser859 by CK1γ2 in vitro and in vivo, which promoted the polyubiquitination and degradation of IRS4 through the ubiquitin/lysosome pathway by the carboxyl terminus of Hsc70-interacting protein(CHIP). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
STUB1
- 
- 