| + |
CSNK2A1 | down-regulates quantity by destabilization 
phosphorylation
|
BMI1 |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277345 |
Ser110 |
SADAANGsNEDRGEV |
Homo sapiens |
|
| pmid |
sentence |
| 28270146 |
Here we report that CK2α, a nuclear serine threonine kinase, phosphorylates BMI1 at Serine 110 as determined by in-vitro/ex-vivo kinase assay and mass spectrometry. e-expression of the phosphorylatable but not non-phosphorylatable BMI1 rescued clonal growth in endogenous BMI1 silenced cancer cells leading us to speculate that CK2α-mediated phosphorylation stabilizes BMI1 and promotes its oncogenic function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Membrane_blebbing | up-regulates activity 
phosphorylation
|
BMI1 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249584 |
Ser316 |
ANRPRKSsVNGSSAT |
|
|
| pmid |
sentence |
| 22505453 |
The polycomb group silencing protein Bmi1 can be phosphorylated by AKT, which enhances its oncogenic potential in PCa. Overexpression of Bmi1 can act in combination with PTEN haploinsufficiency to induce invasive carcinogenic formation in the prostate |
|
| Publications: |
1 |
| + |
AKT1 | up-regulates activity
phosphorylation
|
BMI1 |
0.45 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252559 |
Ser316 |
ANRPRKSsVNGSSAT |
|
|
| pmid |
sentence |
| 22505453 |
The polycomb group silencing protein Bmi1 can be phosphorylated by AKT, which enhances its oncogenic potential in PCa. Overexpression of Bmi1 can act in combination with PTEN haploinsufficiency to induce invasive carcinogenic formation in the prostate |
|
| Publications: |
1 |
| + |
AKT | up-regulates activity
phosphorylation
|
BMI1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249581 |
Ser316 |
ANRPRKSsVNGSSAT |
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 22505453 |
The polycomb group silencing protein Bmi1 can be phosphorylated by AKT, which enhances its oncogenic potential in PCa. Overexpression of Bmi1 can act in combination with PTEN haploinsufficiency to induce invasive carcinogenic formation in the prostate |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT3 | up-regulates activity
phosphorylation
|
BMI1 |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249583 |
Ser316 |
ANRPRKSsVNGSSAT |
|
|
| pmid |
sentence |
| 22505453 |
the polycomb group silencing protein Bmi1 can be phosphorylated by AKT, which enhances its oncogenic potential in PCa. Overexpression of Bmi1 can act in combination with PTEN haploinsufficiency to induce invasive carcinogenic formation in the prostate |
|
| Publications: |
1 |
| + |
AKT2 | up-regulates activity
phosphorylation
|
BMI1 |
0.297 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249582 |
Ser316 |
ANRPRKSsVNGSSAT |
|
|
| pmid |
sentence |
| 22505453 |
the polycomb group silencing protein Bmi1 can be phosphorylated by AKT, which enhances its oncogenic potential in PCa. Overexpression of Bmi1 can act in combination with PTEN haploinsufficiency to induce invasive carcinogenic formation in the prostate |
|
| Publications: |
1 |
| + |
Ub:E2 | up-regulates activity
ubiquitination
|
BMI1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271050 |
|
|
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 |
| + |
BMI1 | form complex 
binding
|
Polycomb repressive complex 1 |
0.787 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266812 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31608994 |
PRC1 has been categorised into canonical and noncanonical/variant PRC1; canonical PRC1 (Morey, Aloia, Cozzuto, Benitah, & Di Croce, 2013) includes chromobox (Cbx) proteins, Ring1, human polyhomeotic homologue protein (Hph) and polycomb ring finger (Pcgf) (Pcgf2/Mel18 and Pcgf4/Bmi1) proteins whereas noncanonical/variant PRC1 involves RING1 and YY1 binding protein (Rybp), Ring1 and Pcgf (Pcgf 1–6) proteins (Wu, Johansen, & Helin, 2013). Figure 3 illustrates the various proteins that form the canonical and noncanonical PRC1. The Ring1 along with Pcgf2/4 forms a core heterodimer which interacts with other accessory components of PRC1 complex through C‐terminal ring finger and WD40 ubiquitin‐like (RAWUL) domains see Figure 4b |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMI1 | down-regulates 
|
NDN |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253386 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24392140 |
In HEK293A cells transfected with luciferase reporter constructs, necdin relieves Bmi1-dependent repression of p16 promoter activity, whereas Bmi1 counteracts necdin-mediated repression of E2F1-dependent Cdk1 promoter activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NDN | down-regulates
|
BMI1 |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253384 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24392140 |
In HEK293A cells transfected with luciferase reporter constructs, necdin relieves Bmi1-dependent repression of p16 promoter activity, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMI1 | down-regulates quantity by repression
transcriptional regulation
|
CDKN2A |
0.47 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259359 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20551323 |
One important pathway in which bmi-1 acts to promote the overall growth of mice and cellular proliferation includes cdkn2a;bmi-1 represses the expression of cdkn2a, which encodes two cyclin-dependent kinase inhibitors, p16ink4a (p16) and p19arf |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMI1 | down-regulates quantity by repression
transcriptional regulation
|
PTEN |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189040 |
|
|
Homo sapiens |
Lymphoma Cell |
| pmid |
sentence |
| 19884659 |
Chromatin immunoprecipitation assays revealed the bmi-1 transcriptionally downregulated expression of the tumor suppressor pten in tumor cells through direct association with the pten locus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Cullin 3-RBX1-Skp1 | up-regulates activity
ubiquitination
|
BMI1 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272661 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15897469 |
BMI1 and MACROH2A1 interact with and are ubiquitinated by the CULLIN3 and SPOP ligase complex. Polyubiquitination of endogenous BMI1 could not be detected, suggesting that only a small amount of the protein undergoes this modification. No significant changes in protein stability were observed, suggesting that ubiquitination serves regulatory functions other than protein degradation of BMI1 and MACROH2A1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMI1 | down-regulates quantity by repression
transcriptional regulation
|
CDKN2A |
0.47 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253385 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24392140 |
In HEK293A cells transfected with luciferase reporter constructs, necdin relieves Bmi1-dependent repression of p16 promoter activity, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBAP2L | up-regulates activity
binding
|
BMI1 |
0.493 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261315 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25185265 |
We identified UBAP2L as a novel BMI1-interacting protein. UBAP2L, BMI1, RNF2, and PHC1 define a novel Polycomb subcomplex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMI1 | up-regulates quantity by expression
transcriptional regulation
|
BMI1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245344 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 23239878 |
Here, we report that BMI1 autoactivates its own promoter via an E-box present in its promoter. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | WNT Signaling |
| + |
BMI1 | down-regulates quantity by repression
transcriptional regulation
|
CDKN2A |
0.47 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166163 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20551323 |
One important pathway in which bmi-1 acts to promote the overall growth of mice and cellular proliferation includes cdkn2a;bmi-1 represses the expression of cdkn2a, which encodes two cyclin-dependent kinase inhibitors, p16ink4a (p16) and p19arf |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SPOP | up-regulates activity
binding
|
BMI1 |
0.409 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272658 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15897469 |
Here, we describe an E3 ubiquitin ligase consisting of SPOP and CULLIN3 that is able to ubiquitinate the PcG protein BMI1 and the variant histone MACROH2A1. To investigate whether BMI1 can form a complex with SPOP and CULLIN3 in vivo, we reconstituted the complex in 293HEK cells. We find that BMI1 readily immunoprecipitates both hemagglutinin (HA)-SPOP and CULLIN3, and, conversely, CULLIN3 immunoprecipitates BMI1 (Fig. 2a). Complex formation depends on the presence of SPOP, in accordance with BMI1 binding to the MATH domain of SPOP (Fig. 1b) and previously published data showing SPOP–CULLIN interaction by means of the BTB/POZ domain of SPOP (30). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
BMI1
- 
- 