+ |
MAPK3 | up-regulates activity
phosphorylation
|
ASB2 |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272241 |
Ser371 |
RIRRSGVsPLHLAAE |
|
|
pmid |
sentence |
24044920 |
Indeed, using mass spectrometry, we showed for the first time that ASB2a is phosphorylated and that phosphorylation of serine-323 (Ser-323) of ASB2a is crucial for the targeting of the actin-binding protein filamin A (FLNa) to degradation. |Moreover, inhibition of the extracellular signal-regulated kinases 1 and 2 (Erk1/2) activity reduced ASB2a-mediated FLNa degradation. |
|
Publications: |
1 |
+ |
MAPK1 | up-regulates activity
phosphorylation
|
ASB2 |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272240 |
Ser371 |
RIRRSGVsPLHLAAE |
|
|
pmid |
sentence |
24044920 |
Indeed, using mass spectrometry, we showed for the first time that ASB2a is phosphorylated and that phosphorylation of serine-323 (Ser-323) of ASB2a is crucial for the targeting of the actin-binding protein filamin A (FLNa) to degradation. |Moreover, inhibition of the extracellular signal-regulated kinases 1 and 2 (Erk1/2) activity reduced ASB2a-mediated FLNa degradation. |
|
Publications: |
1 |
+ |
ERK1/2 | up-regulates activity
phosphorylation
|
ASB2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272239 |
Ser371 |
RIRRSGVsPLHLAAE |
|
|
pmid |
sentence |
24044920 |
Indeed, using mass spectrometry, we showed for the first time that ASB2a is phosphorylated and that phosphorylation of serine-323 (Ser-323) of ASB2a is crucial for the targeting of the actin-binding protein filamin A (FLNa) to degradation. |Moreover, inhibition of the extracellular signal-regulated kinases 1 and 2 (Erk1/2) activity reduced ASB2a-mediated FLNa degradation. |
|
Publications: |
1 |
+ |
ASB2 | up-regulates activity
binding
|
Elongin E3-Cul-5 |
0.628 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271800 |
|
|
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 |
+ |
ASB2 | down-regulates quantity by destabilization
polyubiquitination
|
FLNA |
0.453 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271740 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
18799729 |
ASB2 is the specificity subunit of an E3 ubiquitin ligase complex and is proposed to exert its effects by regulating the turnover of specific proteins; however, no ASB2 substrates had been identified. Here, we report that ASB2 targets the actin-binding proteins filamin A and B for proteasomal degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ASB2 | down-regulates quantity by destabilization
binding
|
FLNB |
0.426 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271795 |
|
|
|
|
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 |