| + |
PCGF2 | down-regulates activity 
binding
|
UBE2I |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-226248 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18211895 |
Based on this finding of interaction between MEL-18 and UBC9, we envisioned a mechanism in which MEL-18 bound to HSF2 inhibits its sumoylation by binding to and inhibiting the activity of UBC9 enzymes that approach HSF2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PCGF2 | down-regulates activity
sumoylation
|
HSF2 |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-226245 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18211895 |
MEL-18, in contrast to the polycomb protein PC2/CBX4, in which SUMO E3 activity stimulates sumoylation of certain proteins, actually functions like an anti-SUMO E3 protein, interacting with both HSF2 and the SUMO E2 UBC9 but acting to inhibit UBC9 activity and thereby decreasing sumoylation of a target protein, in this case that of HSF2. sumoylation of HSF2 is up-regulated during mitosis and is important for the interaction of this factor with a subunit of the condensin complex during the bookmarking process |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PCGF2 | form complex 
binding
|
Polycomb repressive complex 1 |
0.764 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266813 |
|
|
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 |
| + |
Ub:E2 | up-regulates activity 
ubiquitination
|
PCGF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271089 |
|
|
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 |
3.0
PCGF2
- 
- 