+ |
RNF2 | form complex
binding
|
Polycomb repressive complex 1 |
0.821 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266811 |
|
|
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 |
+ |
RNF2 | form complex
binding
|
Noncanonical PRC1 |
0.573 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255277 |
|
|
Mus musculus |
|
pmid |
sentence |
25533466 |
inhibition of adipogenesis does not require the JmjC demethylase domain of FBXL10, but it does require the F-box and leucine-rich repeat domains, which we show recruit a noncanonical polycomb repressive complex 1 (PRC1) containing RING1B, SKP1, PCGF1, and BCOR. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
UBAP2L | up-regulates activity
binding
|
RNF2 |
0.357 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261316 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
25185265 |
UBAP2L associates with BMI1 and RNF2. UBAP2L, BMI1, RNF2, and PHC1 define a novel Polycomb subcomplex |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BCOR | up-regulates activity
binding
|
RNF2 |
0.561 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252241 |
|
|
Homo sapiens |
|
pmid |
sentence |
17296600 |
BcoR and Fbxl10/Jhdm1B are among the most abundant Ring1B/Rnf2 interactors identified with the highest confidence, and their association has been validated by coimmunoprecipitation studies; hence we call this the Fbxl10-BcoR complex. In summary, we have widened the set of multiprotein complexes containing the Polycomb group protein Ring1B/Rnf2. The new interactors contain protein motifs whose enzymatic activities and binding properties would expand the regulatory potential and gene target diversity of Ring1B/Rnf2 complexes in terms of recruitment to and modification of chromatin |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KDM2B | up-regulates activity
binding
|
RNF2 |
0.628 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252242 |
|
|
Homo sapiens |
|
pmid |
sentence |
17296600 |
BcoR and Fbxl10/Jhdm1B are among the most abundant Ring1B/Rnf2 interactors identified with the highest confidence, and their association has been validated by coimmunoprecipitation studies; hence we call this the Fbxl10-BcoR complex. The assembly of Fbxl10-BcoR complex(es), the associations among its various subunits, and its functional significance remain to be characterized but are presently under investigation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
RNF2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271025 |
|
|
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 |