| + |
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 |
| + |
BMPR1B | up-regulates
phosphorylation
|
SMAD1 |
0.628 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52662 |
Ser462 |
GSPHNPIsSVS |
Homo sapiens |
|
| pmid |
sentence |
| 9335504 |
The c terminus of smad1, which is phosphorylated directly by the bmp type i receptor at the ssvs sequence in contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52666 |
Ser463 |
SPHNPISsVS |
Homo sapiens |
|
| pmid |
sentence |
| 9335504 |
The c terminus of smad1, which is phosphorylated directly by the bmp type i receptor at the ssvs sequence in contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52670 |
Ser465 |
HNPISSVs |
Homo sapiens |
|
| pmid |
sentence |
| 9335504 |
The c terminus of smad1, which is phosphorylated directly by the bmp type i receptor at the ssvs sequence in contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187190 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
BMPR1B | up-regulates 
|
SMAD5 |
0.667 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235625 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 10564272 |
We found that both smad6 and smad7 inhibit the activation of smad1 and smad5 by bmpr-ia/alk-3 and bmpr-ib/alk-6, as well as that by alk-2 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BMPR1B | up-regulates activity
phosphorylation
|
SMAD5 |
0.667 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255260 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1A | up-regulates
binding
|
BMPR1B |
0.474 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75649 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10712517 |
Using several complementary approaches, we investigated the formation of homomeric and heteromeric complexes between the two known bmp type i receptors |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1B | up-regulates
phosphorylation
|
SMAD1/5/8 |
0.698 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269846 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9335504 |
The c terminus of smad1, which is phosphorylated directly by the bmp type i receptor at the ssvs sequence in contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1B | up-regulates
phosphorylation
|
SMAD9 |
0.697 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187196 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1B | up-regulates activity
phosphorylation
|
SMAD1 |
0.628 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255265 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1B | up-regulates
phosphorylation
|
SMAD5 |
0.667 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187193 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMHR2 | up-regulates
binding
|
BMPR1B |
0.439 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121596 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14746809 |
See table2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR2 | up-regulates
binding, phosphorylation
|
BMPR1B |
0.608 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75655 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10712517 |
Using several complementary approaches, we investigated the formation of homomeric and heteromeric complexes between the two known bmp type i receptors (br-ia and br-ib) and the bmp type ii receptor (br-ii). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180548 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18756288 |
Bmp ligands bind to the bmp receptors bmpr1 and bmpr2, and bmpr2 then phosphorylates and activates bmpr1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
BMPR2 | up-regulates activity
binding
|
BMPR1B |
0.608 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219291 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 10712517 |
Using several complementary approaches, we investigated the formation of homomeric and heteromeric complexes between the two known bmp type i receptors (br-ia and br-ib) and the bmp type ii receptor (br-ii). |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
GDF5 | up-regulates activity
binding
|
BMPR1B |
0.777 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256483 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 15890363 |
In contrast to other members of the TGF-beta superfamily, GDF-5 shows a pronounced specificity in type I receptor interaction in cross-link experiments binding only to BMP receptor IB (BMPR-IB). In mice, deletion of either GDF-5 or BMPR-IB results in a similar phenotype, indicating that GDF-5 signaling is highly dependent on BMPR-IB. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BMPR1B | up-regulates
|
SMAD1 |
0.628 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235622 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 10564272 |
We found that both smad6 and smad7 inhibit the activation of smad1 and smad5 by bmpr-ia/alk-3 and bmpr-ib/alk-6, as well as that by alk-2 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BMPR1B | up-regulates activity
phosphorylation
|
SMAD9 |
0.697 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255264 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMAD7 | down-regulates 
|
BMPR1B |
0.687 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236864 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 10564272 |
We found that both smad6 and smad7 inhibit the activation of smad1 and smad5 by bmpr-ia/alk-3 and bmpr-ib/alk-6, as well as that by alk-2 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
NOG | down-regulates activity 
binding
|
BMPR1B |
0.584 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192802 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Noggin binds the domain that is re-quired for bmp-7 to interact with bmp type i and type ii receptors.Noggin Inhibits bmp by blocking the molecular interfaces of the binding epitopes for both type i and type ii receptors (pmid 12478285) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1B | form complex 
binding
|
BMPR1A/1B/2 |
0.541 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-33431 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7791754 |
Using several complementary approaches, we investigated the formation of homomeric and heteromeric complexes between the two known bmp type i receptors (br-ia and br-ib) and the bmp type ii receptor (br-ii). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
BMPR1B
- 
- 