+ |
ELOC | up-regulates
phosphorylation
|
H1-1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-166120 |
Ser183 |
KPKKVAKsPAKAKAV |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
20551309 |
Our results also show the potential function of p-tefb phosphorylation of h1, namely, to increase h1 dissociation from actively transcribed dna. P-tefb preferentially phosphorylates the ser-183 phosphorylation site of histone h1.1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ELOC | form complex
binding
|
BAF250b E3 ligase |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271438 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
20086098 |
In the present work, we show that BAF250 associates with elongin C (Elo C), cullin 2 (Cul2), and Roc1 to form an E3 ubiquitin ligase. BAF250 forms an E3 ubiquitin ligase with Elo B/C, Cul2, and Roc1 that targets histone H2B. H2B-Ub has been shown to be required for transcriptional activation in vitro |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ELOC | down-regulates
ubiquitination
|
NOTCH4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176779 |
|
|
Homo sapiens |
|
pmid |
sentence |
22001063 |
Using proteomic techniques, several components of the elongin c complex were identified as candidate notch4(icd) interactors. Elongin c complexes can function as ubiquitin ligases capable of regulating proteasomal degradation of specific protein substrates. Our studies indicate that ectopic elongin c expression stimulates notch4(icd) degradation and inhibits its transcriptional activity in human kidney tubule hk11 cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Hindbrain |
+ |
ELOC | form complex
binding
|
Elongin E3-Cul-5 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271797 |
|
|
Mus musculus |
C2C12 Cell |
pmid |
sentence |
19300455 |
Here, we provide the first evidence that a novel ASB2 isoform, ASB2beta, is important for muscle differentiation. ASB2beta is expressed in muscle cells during embryogenesis and in adult tissues. ASB2beta is part of an active E3 ubiquitin ligase complex and targets the actin-binding protein filamin B (FLNb) for proteasomal degradation. Altogether, our results indicated that ASB2β can assemble with elongin B, elongin C, Cullin 5 and Rbx2 to reconstitute an active E3 ubiquitin ligase complex.ASB2β induces polyubiquitylation of FLNb. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
ELOC | form complex
binding
|
VCB-Cul2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271518 |
|
|
Homo sapiens |
|
pmid |
sentence |
11574546 |
The von Hippel-Lindau tumor-suppressor protein (pVHL) forms a protein complex (VCB-Cul2) with elongin C, elongin B, Cul-2, and Rbx1, which functions as a ubiquitin-protein ligase (E3). The alpha-subunits of the hypoxia-inducible factors have been identified as targets for the VCB-Cul2 ubiquitin ligase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |