| + |
BMPR1B | up-regulates activity 
phosphorylation
|
STAMBP |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250596 |
Ser2 |
sDHGDVSL |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11483516 |
BMP type I receptor activation stimulates AMSH phosphorylation | The exact position of phosphoserine residues in four phosphopeptides was identified by Edman degradation analysis; spot a for Ser243, Ser245 and Ser247, spot b for Ser2, and spots c and d for Ser48. To confirm the position of the phosphoserine residues, the serine residue(s) in each phosphopeptide was replaced by alanine residues. Then, each mutant as well as wild‐type AMSH was transfected into COS7 cells in the absence or presence of caALK6, and tryptic phosphopeptide mapping of each mutant was performed. As seen in Figure 7, each spot corresponding to the phosphopeptide containing phosphoserine disappeared in the tryptic phosphopeptide mapping. | Thus, AMSH promotes BMP signaling by negatively regulating the function of I‐Smads. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250597 |
Ser243 |
SLKPGALsNSESIPT |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11483516 |
BMP type I receptor activation stimulates AMSH phosphorylation | The exact position of phosphoserine residues in four phosphopeptides was identified by Edman degradation analysis; spot a for Ser243, Ser245 and Ser247, spot b for Ser2, and spots c and d for Ser48. To confirm the position of the phosphoserine residues, the serine residue(s) in each phosphopeptide was replaced by alanine residues. Then, each mutant as well as wild‐type AMSH was transfected into COS7 cells in the absence or presence of caALK6, and tryptic phosphopeptide mapping of each mutant was performed. As seen in Figure 7, each spot corresponding to the phosphopeptide containing phosphoserine disappeared in the tryptic phosphopeptide mapping. | Thus, AMSH promotes BMP signaling by negatively regulating the function of I‐Smads. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250598 |
Ser245 |
KPGALSNsESIPTID |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11483516 |
BMP type I receptor activation stimulates AMSH phosphorylation | The exact position of phosphoserine residues in four phosphopeptides was identified by Edman degradation analysis; spot a for Ser243, Ser245 and Ser247, spot b for Ser2, and spots c and d for Ser48. To confirm the position of the phosphoserine residues, the serine residue(s) in each phosphopeptide was replaced by alanine residues. Then, each mutant as well as wild‐type AMSH was transfected into COS7 cells in the absence or presence of caALK6, and tryptic phosphopeptide mapping of each mutant was performed. As seen in Figure 7, each spot corresponding to the phosphopeptide containing phosphoserine disappeared in the tryptic phosphopeptide mapping. | Thus, AMSH promotes BMP signaling by negatively regulating the function of I‐Smads. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250599 |
Ser247 |
GALSNSEsIPTIDGL |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11483516 |
BMP type I receptor activation stimulates AMSH phosphorylation | The exact position of phosphoserine residues in four phosphopeptides was identified by Edman degradation analysis; spot a for Ser243, Ser245 and Ser247, spot b for Ser2, and spots c and d for Ser48. To confirm the position of the phosphoserine residues, the serine residue(s) in each phosphopeptide was replaced by alanine residues. Then, each mutant as well as wild‐type AMSH was transfected into COS7 cells in the absence or presence of caALK6, and tryptic phosphopeptide mapping of each mutant was performed. As seen in Figure 7, each spot corresponding to the phosphopeptide containing phosphoserine disappeared in the tryptic phosphopeptide mapping. | Thus, AMSH promotes BMP signaling by negatively regulating the function of I‐Smads. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250600 |
Ser48 |
VEIIRMAsIYSEEGN |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11483516 |
BMP type I receptor activation stimulates AMSH phosphorylation | The exact position of phosphoserine residues in four phosphopeptides was identified by Edman degradation analysis; spot a for Ser243, Ser245 and Ser247, spot b for Ser2, and spots c and d for Ser48. To confirm the position of the phosphoserine residues, the serine residue(s) in each phosphopeptide was replaced by alanine residues. Then, each mutant as well as wild‐type AMSH was transfected into COS7 cells in the absence or presence of caALK6, and tryptic phosphopeptide mapping of each mutant was performed. As seen in Figure 7, each spot corresponding to the phosphopeptide containing phosphoserine disappeared in the tryptic phosphopeptide mapping. | Thus, AMSH promotes BMP signaling by negatively regulating the function of I‐Smads. |
|
| Publications: |
5 |
Organism: |
Chlorocebus Aethiops |
| + |
SMURF2 | down-regulates quantity by destabilization 
polyubiquitination
|
STAMBP |
0.546 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272951 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14755250 |
RNF11 recruits AMSH to Smurf2 E3 ligase. Smurf2 promotes ubiquitination of AMSH in the presence of wt RNF11. Previously, we have shown that RNF11 interacts with the HECT-type E3 ligases AIP4 and Smurf2. Here, we show that RNF11 binds to AMSH in mammalian cells and that this interaction is independent of the RNF11 RING-finger domain and the PY motif. Our results also demonstrate that AMSH is ubiquitinated by Smurf2 E3 ligase in the presence of RNF11 and that a consequent reduction in its steady-state level requires both RNF11 and Smurf2. RNF11 therefore recruits AMSH to Smurf2 for ubiquitination, leading to its degradation by the 26S proteasome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF11 | down-regulates quantity by destabilization
binding
|
STAMBP |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272953 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14755250 |
RNF11 recruits AMSH to Smurf2 E3 ligase. Smurf2 promotes ubiquitination of AMSH in the presence of wt RNF11. Previously, we have shown that RNF11 interacts with the HECT-type E3 ligases AIP4 and Smurf2. Here, we show that RNF11 binds to AMSH in mammalian cells and that this interaction is independent of the RNF11 RING-finger domain and the PY motif. Our results also demonstrate that AMSH is ubiquitinated by Smurf2 E3 ligase in the presence of RNF11 and that a consequent reduction in its steady-state level requires both RNF11 and Smurf2. RNF11 therefore recruits AMSH to Smurf2 for ubiquitination, leading to its degradation by the 26S proteasome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
STAMBP
- 
- 