+ |
HERC2 | down-regulates quantity by destabilization
polyubiquitination
|
NEURL4 |
0.467 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272910 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
22261722 |
Here we used interaction proteomics to identify the E3 ligase HERC2 and the neuralized homologue NEURL4 as novel interaction partners of the centrosomal protein CP110.NEURL4 is a substrate of HERC2, and together these results indicate that the NEURL4-HERC2 complex participates in the ubiquitin-dependent regulation of centrosome architecture. In further support of the possibility that NEURL4 is regulated by proteasomal degradation, we detected robust ubiquitylation of a FLAG-NEURL4 protein in HEK293T cells (Fig. 5B). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272921 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
22261722 |
NEURL4 is a substrate of HERC2, and together these results indicate that the NEURL4-HERC2 complex participates in the ubiquitin-dependent regulation of centrosome architecture. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
HERC2 | down-regulates quantity
ubiquitination
|
USP20 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278692 |
|
|
Homo sapiens |
|
pmid |
sentence |
25326330 |
HERC2 promotes USP20 degradation.|Under unperturbed condition, HERC2 ubiquitinates USP20 and promotes ubiquitination mediated proteasomal degradation of USP20, regulating the status of K48 linked polyubiquitination of CLASPIN and ensuring appropriate protein levels of CLASPIN during the S-phase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HERC2 | down-regulates quantity by destabilization
ubiquitination
|
BRCA1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278813 |
|
|
Homo sapiens |
|
pmid |
sentence |
20631078 |
HERC2 ubiquitinates BRCA1; this reaction depends on Cys(4762) of HERC2, the catalytic ubiquitin binding site, and the degron of BRCA1.|Significantly, HERC2 depletion antagonizes the effects of BARD1 depletion by restoring BRCA1 expression and G(2)-M checkpoint activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HERC2 | down-regulates
ubiquitination
|
XPA |
0.392 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164595 |
|
|
Homo sapiens |
|
pmid |
sentence |
20304803 |
Herc2 may ubiquitinate xpa and thus target it for proteolytic degradation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HERC2 | down-regulates quantity by destabilization
polyubiquitination
|
USP20 |
0.378 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272820 |
|
|
in vitro |
|
pmid |
sentence |
25355518 |
USP20 is regulated by HERC2 following DNA damage or replication stress.The HECT domain of WT HERC but not the catalytic inactive mutant (CA) ubiquitinated USP20 in vitro (Figure (Figure4G).4G). Taken together, these results suggested that HERC2 functions as an E3 ligase of USP20 and negatively regulates USP20 in unstressed cells. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
HERC2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271292 |
|
|
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 |