| + |
APC-c | down-regulates quantity by destabilization 
polyubiquitination
|
DTYMK |
0.284 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272653 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16103219 |
We demonstrate that TMPK is recognized and degraded by APC/C-Cdc20/Cdh1-mediated pathways from mitosis to the early G1 phase, whereas TK1 is targeted for degradation by APC/C-Cdh1 after mitotic exit. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MCC | down-regulates activity
binding
|
APC-c |
0.799 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265977 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25092294 |
The mitotic (or spindle assembly) checkpoint system delays anaphase until all chromosomes are correctly attached to the mitotic spindle. When the checkpoint is active, a Mitotic Checkpoint Complex (MCC) assembles and inhibits the ubiquitin ligase Anaphase-Promoting Complex/Cyclosome (APC/C). MCC is composed of the checkpoint proteins Mad2, BubR1, and Bub3 associated with the APC/C activator Cdc20. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
KIF2C |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266111 |
|
|
in vitro |
|
| pmid |
sentence |
| 24510915 |
Biochemical studies on the kinesins confirmed KIFC1, KIF18A, KIF2C, and KIF4A as APC/C substrates. Furthermore, we showed that the APC/CCDH1-dependent degradation of KIFC1 regulates the bipolar spindle formation and proper cell division. Our in vitro degradation assays showed a time-dependent degradation for four of the five potential substrates tested: KIF18A, KIF2C, KIFC1 and KIF4A were readily degraded in vitro, however remained stable in the presence of either APC/C inhibitor (Fig(Fig4A4A and Supplementary Fig S3A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276864 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25504441 |
Our studies suggest new mechanisms by which Plk1 regulates MCAK: the degradation of MCAK is controlled by Plk1 phosphorylation on S621, whereas its activity is modulated by Plk1 phosphorylation on S632/S633 in mitosis.We have recently shown that S621 in MCAK is the major phosphorylation site of Plk1, which is responsible for regulating MCAK's degradation by promoting the association of MCAK with APC/CCdc20. In the present study, we have addressed another two residues phosphorylated by Plk1, namely S632/S633 in the C-terminus of MCAK. Our data suggest that Plk1 phosphorylates S632/S633 and regulates its catalytic activity in mitosis. This phosphorylation is required for proper spindle assembly during early phases of mitosis. |
|
| Publications: |
2 |
Organism: |
In Vitro, Homo Sapiens |
| + |
ANAPC4 | form complex 
binding
|
APC-c |
0.906 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252004 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known to catalyse ubiquitylation reactions, and it contains more than a dozen subunits that assemble into a large 1.5-MDa complex. |
|
| Publications: |
1 |
| + |
ANAPC7 | form complex
binding
|
APC-c |
0.847 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252007 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known to catalyse ubiquitylation reactions, and it contains more than a dozen subunits that assemble into a large 1.5-MDa complex. |
|
| Publications: |
1 |
| + |
ANAPC10 | form complex
binding
|
APC-c |
0.921 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252009 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known to catalyse ubiquitylation reactions, and it contains more than a dozen subunits that assemble into a large 1.5-MDa complex. |
|
| Publications: |
1 |
| + |
CDC20 | up-regulates activity 
binding
|
APC-c |
0.881 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272880 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23979597 |
We showed that PHF8 interacts with the CDC20-containing APC (APC(cdc20)) primarily during mitosis. we demonstrate that mutations of the LXPKXLF motif abrogate polyubiquitylation of PHF8 by the APC. APC substrates are typically cell cycle regulators, and consistent with this, the loss of PHF8 leads to prolonged G2 phase and defective mitosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252014 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
In addition to E2 enzymes, APC/C activity is also strictly dependent on one of several co-activator proteins that associate with APC/C during specific periods of the cell cycle. The best studied of these are Cdc20 and Cdh1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272896 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23287467 |
Here, we show that human REV1 undergoes proteosomal degradation mediated by the E3 ubiquitin ligase known as anaphase-promoting complex (APC). REV1 associates with APC. Overexpression of APC coactivator CDH1 or CDC20 promotes polyubiquitination and proteosomal degradation of REV1. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
CDR2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252024 |
|
|
|
|
| pmid |
sentence |
| 20383333 |
Here we find that cdr2 is cell cycle regulated in tumor cells with protein levels peaking in mitosis. As cells exit mitosis, cdr2 is ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) and rapidly degraded by the proteasome. Previously we showed that cdr2 binds to the oncogene c-myc, and here we extend this observation to show that cdr2 and c-myc interact to synergistically regulate c-myc-dependent transcription during passage through mitosis. |
|
| Publications: |
1 |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
ANLN |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272655 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16040610 |
Ubiquitination of anillin required a destruction-box and was mediated by Cdh1, an activator of APC/C. Overexpression of Cdh1 reduced the levels of anillin, whereas inactivation of APC/C(Cdh1) increased the half-life of anillin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
APC-c |
0.888 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272725 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22086178 |
Cdc20 is a co-activator of the anaphase-promoting complex/cyclosome (APC/C complex), which recruits substrates at particular phases of the cell cycle and mediates their degradation. Overexpression of Cdc20 resulted in decreased levels of both endogenous Sp100 protein and overexpressed Sp100 mRNA in HEK 293 cells. Our results suggested that sp100 is a novel substrate of Cdc20 and it is degraded by the ubiquitination pathway. The intact D-box of Sp100 was necessary for this process. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
IRS2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272196 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 32554797 |
We conducted an unbiased proteomic screen to uncover novel substrates of the Anaphase Promoting Complex/Cyclosome (APC/C), a ubiquitin ligase that controls the abundance of key cell cycle regulators. We found that IRS2 levels are regulated by APC/C activity and that IRS2 is a direct APC/C target in G1 Consistent with the APC/C's role in degrading cell cycle regulators. Consistent with this observation, we found that APC/C inhibition decreased the polyubiquitylation of HA-tagged IRS2 in HeLa cells treated with MG132 (Fig. 2G). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
USP37 |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265048 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21596315 |
USP37 is ubiquitinated by APCCDH1 in late mitosis and early G1 phase||Inactive USP37 now becomes a substrate for APCCDH1, undergoing K11-linked polyubiquitination and proteasomal degradation. Elimination of USP37 ensures that it does not antagonize APC/C substrate degradation during mitosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDH1 | up-regulates activity
binding
|
APC-c |
0.378 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274058 |
|
|
|
|
| pmid |
sentence |
| 18662541 |
In early mitosis, APC/C is activated through binding to Cdc20, and in late M, Cdc20 is replaced by Cdh1, the second activator of APC/C. |
|
| Publications: |
1 |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
KIFC1 |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266109 |
|
|
in vitro |
|
| pmid |
sentence |
| 24510915 |
Biochemical studies on the kinesins confirmed KIFC1, KIF18A, KIF2C, and KIF4A as APC/C substrates. Furthermore, we showed that the APC/CCDH1-dependent degradation of KIFC1 regulates the bipolar spindle formation and proper cell division. Our in vitro degradation assays showed a time-dependent degradation for four of the five potential substrates tested: KIF18A, KIF2C, KIFC1 and KIF4A were readily degraded in vitro, however remained stable in the presence of either APC/C inhibitor (Fig(Fig4A4A and Supplementary Fig S3A). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
SKIL |
0.319 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272622 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11741538 |
We demonstrate that the anaphase-promoting complex (APC) is a ubiquitin ligase required for the destruction of SnoN and that the APC pathway is regulated by TGF-beta. The destruction box of SnoN is required for its degradation in response to TGF-beta signaling. Furthermore, the APC activator CDH1 and Smad3 synergistically regulate SnoN degradation. Under these circumstances, CDH1 forms a quaternary complex with SnoN, Smad3, and APC. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
PSMD4 |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272750 |
|
|
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 |
| + |
APC-c | up-regulates activity
binding
|
CDC6 |
0.522 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271386 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10995389 |
Furthermore, APC, in association with CDH1, ubiquitinates CDC6 in vitro, and both APC and CDH1 are required and limiting for CDC6 proteolysis in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ANAPC13 | form complex
binding
|
APC-c |
0.839 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252012 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known to catalyse ubiquitylation reactions, and it contains more than a dozen subunits that assemble into a large 1.5-MDa complex. |
|
| Publications: |
1 |
| + |
ANAPC2 | form complex
binding
|
APC-c |
0.879 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252002 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known to catalyse ubiquitylation reactions, and it contains more than a dozen subunits that assemble into a large 1.5-MDa complex. |
|
| Publications: |
1 |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
CCNA2 |
0.575 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265050 |
|
|
|
|
| pmid |
sentence |
| 21596315 |
Complexed with the activator proteins CDC20 or CDH1 (Fang et al., 1998, Visintin et al., 1997), the APC/C recognizes, ubiquitinates, and targets for proteasomal degradation a multitude of cell cycle regulators containing KEN or D box degrons, including securin, cyclin A, and cyclin B. |
|
| Publications: |
1 |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
AURKA |
0.467 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272612 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 12023018 |
We previously showed that human Aurora-A is turned over through the anaphase promoting complex/cyclosome (APC/C)–ubiquitin–proteasome pathway. The association of two distinct WD40 repeat proteins known as Cdc20 and Cdh1, respectively, sequentially activates the APC/C. The present study shows that Aurora-A degradation is dependent on hCdh1 in vivo, not on hCdc20, and that Aurora-A is targeted for proteolysis through distinct structural features of the destruction box, the KEN box motifs and its kinase activity. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
TK1 |
0.247 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272946 |
|
|
in vitro |
|
| pmid |
sentence |
| 14701726 |
We show that hTK1 is degraded via a ubiquitin-proteasome pathway in mammalian cells and that anaphase-promoting complex/cyclosome (APC/C) activator Cdh1 is not only a necessary but also a rate-limiting factor for mitotic degradation of hTK1. By in vitro ubiquitinylation assays, we demonstrated that hTK1 is targeted for degradation by the APC/C-Cdh1 ubiquitin ligase dependent on this KEN box motif. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
CCNB1 |
0.636 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265051 |
|
|
|
|
| pmid |
sentence |
| 21596315 |
Complexed with the activator proteins CDC20 or CDH1 (Fang et al., 1998, Visintin et al., 1997), the APC/C recognizes, ubiquitinates, and targets for proteasomal degradation a multitude of cell cycle regulators containing KEN or D box degrons, including securin, cyclin A, and cyclin B. |
|
| Publications: |
1 |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
CLSPN |
0.258 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274056 |
|
|
|
|
| pmid |
sentence |
| 18662541 |
Claspin Is Degraded in G0 and G1 via the APC/CCdh1 Ubiquitin Ligase |
|
| Publications: |
1 |
| + |
ANAPC1 | form complex
binding
|
APC-c |
0.884 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252001 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known to catalyse ubiquitylation reactions, and it contains more than a dozen subunits that assemble into a large 1.5-MDa complex. |
|
| Publications: |
1 |
| + |
ANAPC11 | form complex
binding
|
APC-c |
0.87 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252010 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known to catalyse ubiquitylation reactions, and it contains more than a dozen subunits that assemble into a large 1.5-MDa complex. |
|
| Publications: |
1 |
| + |
FZR1 | up-regulates activity
binding
|
APC-c |
0.856 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272611 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 12023018 |
We previously showed that human Aurora-A is turned over through the anaphase promoting complex/cyclosome (APC/C)–ubiquitin–proteasome pathway. The association of two distinct WD40 repeat proteins known as Cdc20 and Cdh1, respectively, sequentially activates the APC/C. The present study shows that Aurora-A degradation is dependent on hCdh1 in vivo, not on hCdc20, and that Aurora-A is targeted for proteolysis through distinct structural features of the destruction box, the KEN box motifs and its kinase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252015 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
In addition to E2 enzymes, APC/C activity is also strictly dependent on one of several co-activator proteins that associate with APC/C during specific periods of the cell cycle. The best studied of these are Cdc20 and Cdh1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272897 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23287467 |
Here, we show that human REV1 undergoes proteosomal degradation mediated by the E3 ubiquitin ligase known as anaphase-promoting complex (APC). REV1 associates with APC. Overexpression of APC coactivator CDH1 or CDC20 promotes polyubiquitination and proteosomal degradation of REV1. |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops, , Homo Sapiens |
| + |
CDC26 | form complex
binding
|
APC-c |
0.855 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252011 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known to catalyse ubiquitylation reactions, and it contains more than a dozen subunits that assemble into a large 1.5-MDa complex. |
|
| Publications: |
1 |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
KIF18A |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266110 |
|
|
in vitro |
|
| pmid |
sentence |
| 24510915 |
Biochemical studies on the kinesins confirmed KIFC1, KIF18A, KIF2C, and KIF4A as APC/C substrates. Furthermore, we showed that the APC/CCDH1-dependent degradation of KIFC1 regulates the bipolar spindle formation and proper cell division. Our in vitro degradation assays showed a time-dependent degradation for four of the five potential substrates tested: KIF18A, KIF2C, KIFC1 and KIF4A were readily degraded in vitro, however remained stable in the presence of either APC/C inhibitor (Fig(Fig4A4A and Supplementary Fig S3A). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ANAPC5 | form complex
binding
|
APC-c |
0.925 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252005 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known to catalyse ubiquitylation reactions, and it contains more than a dozen subunits that assemble into a large 1.5-MDa complex. |
|
| Publications: |
1 |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
CCNF |
0.481 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266362 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27653696 |
We show that cyclin F, a cell-cycle-regulated substrate receptor (F-box protein) for the SCF, is targeted for degradation by APC/C. Furthermore, we establish that Cdh1 is itself a substrate of SCF(cyclin F). Cyclin F loss impairs Cdh1 degradation and delays S-phase entry, and this delay is reversed by simultaneous removal of Cdh1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
KIF4A |
0.284 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266112 |
|
|
in vitro |
|
| pmid |
sentence |
| 24510915 |
Biochemical studies on the kinesins confirmed KIFC1, KIF18A, KIF2C, and KIF4A as APC/C substrates. Furthermore, we showed that the APC/CCDH1-dependent degradation of KIFC1 regulates the bipolar spindle formation and proper cell division. Our in vitro degradation assays showed a time-dependent degradation for four of the five potential substrates tested: KIF18A, KIF2C, KIFC1 and KIF4A were readily degraded in vitro, however remained stable in the presence of either APC/C inhibitor (Fig(Fig4A4A and Supplementary Fig S3A). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CDC23 | form complex
binding
|
APC-c |
0.918 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252008 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known to catalyse ubiquitylation reactions, and it contains more than a dozen subunits that assemble into a large 1.5-MDa complex. |
|
| Publications: |
1 |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
PHF8 |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272881 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23979597 |
We showed that PHF8 interacts with the CDC20-containing APC (APC(cdc20)) primarily during mitosis. we demonstrate that mutations of the LXPKXLF motif abrogate polyubiquitylation of PHF8 by the APC. APC substrates are typically cell cycle regulators, and consistent with this, the loss of PHF8 leads to prolonged G2 phase and defective mitosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
PPM1D |
0.309 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275492 |
|
|
|
|
| pmid |
sentence |
| 33309518 |
Phosphorylation of multiple residues in the catalytic domain of PPM1D during mitosis, including Ser40 by Cyclin-dependent kinase 1 (CDK1), leads to ubiquitination of PPM1D and subsequent proteasomal degradation by Adenomatous polyposis coli (APC) and cell-division cycle protein 20 (CDC20) |
|
| Publications: |
1 |
| + |
UBE2S | up-regulates activity
binding
|
APC-c |
0.682 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265080 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19822757 |
Here, we identify the highly conserved Ube2S as a regulator of human and Drosophila APC/C. Ube2S functions as a K11-specific chain elongating E2 of APC/C, which depends on chain initiation by UbcH10. Together, UbcH10 and Ube2S are required for the degradation of all APC/C substrates tested so far, spindle formation, and progression of cells through mitosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC16 | form complex
binding
|
APC-c |
0.923 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252006 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known to catalyse ubiquitylation reactions, and it contains more than a dozen subunits that assemble into a large 1.5-MDa complex. |
|
| Publications: |
1 |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
PFKFB3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271435 |
|
|
Homo sapiens |
SH-SY5Y Cell |
| pmid |
sentence |
| 20080744 |
We have recently discovered that the glycolysis-promoting enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, isoform 3 (PFKFB3), is degraded by the E3 ubiquitin ligase APC/C-Cdh1, which also degrades cell-cycle proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC27 | form complex
binding
|
APC-c |
0.895 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252003 |
|
|
|
|
| pmid |
sentence |
| 16896351 |
The anaphase promoting complex/cyclosome (APC/C) is a ubiquitin ligase that has essential functions in and outside the eukaryotic cell cycle. It is the most complex molecular machine that is known to catalyse ubiquitylation reactions, and it contains more than a dozen subunits that assemble into a large 1.5-MDa complex. |
|
| Publications: |
1 |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
REV1 |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272894 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23287467 |
Here, we show that human REV1 undergoes proteosomal degradation mediated by the E3 ubiquitin ligase known as anaphase-promoting complex (APC). REV1 associates with APC. Overexpression of APC coactivator CDH1 or CDC20 promotes polyubiquitination and proteosomal degradation of REV1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272895 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23287467 |
Here, we show that human REV1 undergoes proteosomal degradation mediated by the E3 ubiquitin ligase known as anaphase-promoting complex (APC). REV1 associates with APC. Overexpression of APC coactivator CDH1 or CDC20 promotes polyubiquitination and proteosomal degradation of REV1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
PTTG1 |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265049 |
|
|
|
|
| pmid |
sentence |
| 21596315 |
Complexed with the activator proteins CDC20 or CDH1 (Fang et al., 1998, Visintin et al., 1997), the APC/C recognizes, ubiquitinates, and targets for proteasomal degradation a multitude of cell cycle regulators containing KEN or D box degrons, including securin, cyclin A, and cyclin B. |
|
| Publications: |
1 |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
FBXW5 |
0.423 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275477 |
|
|
|
|
| pmid |
sentence |
| 21725316 |
We show that FBXW5 levels are controlled by the anaphase-promoting (APC/C) complex, which targets FBXW5 for degradation during mitosis and G1, thereby helping to reset the centrosome duplication machinery. |
|
| Publications: |
1 |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
MOAP1 |
0.245 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272912 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22529100 |
MOAP-1 is an APC/CCdh1 substrate. Here, we identify MOAP-1 as a novel APC/CCdh1 substrate. MOAP-1 is degraded during G1 by APC/CCdh1, and this degradation is inhibited by Trim39 acting on the APC/C. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APC-c | up-regulates 
|
Mitotic_checkpoint |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265978 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25092294 |
We then found that the joint action of TRIP13 and p31comet also promotes MCC disassembly, releases APC/C from checkpoint inhibition, and inactivates the mitotic checkpoint. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
PNN |
0.205 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272201 |
|
|
Homo sapiens |
Pancreatic Ductal Adenocarcinoma Cell |
| pmid |
sentence |
| 32203416 |
Apo-PIWIL1 functions as a co-activator for APC/C ubiquitin ligase. Here, we show that in the absence of piRNAs, human PIWIL1 in PDAC functions as an oncoprotein by activating the anaphase promoting complex/cyclosome (APC/C) E3 complex, which then targets a critical cell adhesion-related protein, Pinin, to enhance PDAC metastasis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIWIL1 | up-regulates
binding
|
APC-c |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272202 |
|
|
Homo sapiens |
Pancreatic Ductal Adenocarcinoma Cell |
| pmid |
sentence |
| 32203416 |
PIWIL1 leads to the constitutive activation of APC/C in PDAC cells. Here, we show that in the absence of piRNAs, human PIWIL1 in PDAC functions as an oncoprotein by activating the anaphase promoting complex/cyclosome (APC/C) E3 complex, which then targets a critical cell adhesion-related protein, Pinin, to enhance PDAC metastasis. Collectively, these results demonstrate that Pinin is an authentic substrate of APC/CPIWIL1 in PDAC cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
APC-c
CPX-1860