+ |
UBR5 | down-regulates quantity by destabilization
polyubiquitination
|
SOX2 |
0.258 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277446 |
Lys115 |
YKYRPRRkTKTLMKK |
Homo sapiens |
Esophageal Squamous Cell Carcinoma Cell Line |
pmid |
sentence |
30894683 |
We identified UBR5 as a major ubiquitin E3 ligase that induces SOX2 degradation through ubiquitinating SOX2 at lysine 115. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
UBR5 | down-regulates quantity by destabilization
polyubiquitination
|
PAIP2 |
0.457 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272648 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
16601676 |
We demonstrate a mechanism for this co-regulation that involves an E3 ubiquitin ligase, EDD, which targets Paip2 for degradation. PABP depletion by RNA interference (RNAi) causes co-depletion of Paip2 protein without affecting Paip2 mRNA levels. Upon PABP knockdown, Paip2 interacts with EDD, which leads to Paip2 ubiquitination. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
UBR5 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271299 |
|
|
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 |
+ |
UBR5 | down-regulates quantity by destabilization
polyubiquitination
|
TOPBP1 |
0.474 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272667 |
|
|
in vitro |
|
pmid |
sentence |
11714696 |
Using an in vitro reconstitution, specific E2 (ubiquitin-conjugating) enzymes (human UbcH4, UbcH5B, and UbcH5C) transferred ubiquitin molecules to hHYD, leading to the ubiquitination of TopBP1. TopBP1 was usually ubiquitinated and degraded by the proteosome, whereas X-irradiation diminished the ubiquitination of TopBP1 probably via the phosphorylation, resulting in the stable colocalization of up-regulated TopBP1 with gamma-H2AX nuclear foci in DNA breaks. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
UBR5 | down-regulates quantity by destabilization
ubiquitination
|
PCK1 |
0.313 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267600 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21726808 |
Acetylation Regulates Gluconeogenesis by Promoting PEPCK1 Degradation via Recruiting the UBR5 Ubiquitin Ligase |UBR5 ubiquitinates the acetylated PEPCK1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
UBR5 | form complex
binding
|
EDVP |
0.393 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271790 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19287380 |
We named this E3 ligase complex containing EDD, DDB1 and VPRBP proteins as EDVP complex to distinguish it from the previously identified Cul4-Roc1-DDB1-VPRBP E3 ligase complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
UBR5 | down-regulates quantity
ubiquitination
|
RNF168 |
0.454 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266782 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
22884692 |
Here, we show that TRIP12 and UBR5, two HECT domain ubiquitin E3 ligases, control accumulation of RNF168, a rate-limiting component of a pathway that ubiquitylates histones after DNA breakage. We find that RNF168 can be saturated by increasing amounts of DSBs. Depletion of TRIP12 and UBR5 allows accumulation of RNF168 to supraphysiological levels, followed by massive spreading of ubiquitin conjugates and hyperaccumulation of ubiquitin-regulated genome caretakers such as 53BP1 and BRCA1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
UBE2D3 | up-regulates activity
ubiquitination
|
UBR5 |
0.475 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272669 |
|
|
in vitro |
|
pmid |
sentence |
11714696 |
Using an in vitro reconstitution, specific E2 (ubiquitin-conjugating) enzymes (human UbcH4, UbcH5B, and UbcH5C) transferred ubiquitin molecules to hHYD, leading to the ubiquitination of TopBP1. TopBP1 was usually ubiquitinated and degraded by the proteosome, whereas X-irradiation diminished the ubiquitination of TopBP1 probably via the phosphorylation, resulting in the stable colocalization of up-regulated TopBP1 with gamma-H2AX nuclear foci in DNA breaks. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
TCEA1 | up-regulates
binding
|
UBR5 |
0.364 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170258 |
|
|
Homo sapiens |
|
pmid |
sentence |
21127351 |
We show that the e3 ubiquitin ligase ubr5 associates with the cdk9 subunit of positive transcription elongation factor b to mediate its polyubiquitination in human cells. Tfiis also binds ubr5 to stimulate cdk9 polyubiquitination. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
UBE2D2 | up-regulates activity
ubiquitination
|
UBR5 |
0.522 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272668 |
|
|
in vitro |
|
pmid |
sentence |
11714696 |
Using an in vitro reconstitution, specific E2 (ubiquitin-conjugating) enzymes (human UbcH4, UbcH5B, and UbcH5C) transferred ubiquitin molecules to hHYD, leading to the ubiquitination of TopBP1. TopBP1 was usually ubiquitinated and degraded by the proteosome, whereas X-irradiation diminished the ubiquitination of TopBP1 probably via the phosphorylation, resulting in the stable colocalization of up-regulated TopBP1 with gamma-H2AX nuclear foci in DNA breaks. |
|
Publications: |
1 |
Organism: |
In Vitro |