| + |
BMPR1A/1B/2 | up-regulates 
phosphorylation
|
SMAD1 |
0.679 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-210079 |
Ser463 |
SPHNPISsVS |
Homo sapiens |
|
| pmid |
sentence |
| 9136927 |
Here, we report that bmp receptors phosphorylate and activate smad1 directly. Phosphorylation of smad1 in vivo involves serines in the carboxy-terminal motif ssxs. These residues are phosphorylated directly by a bmp type i receptor in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249648 |
Ser465 |
HNPISSVs |
Homo sapiens |
|
| pmid |
sentence |
| 9136927 |
Here, we report that bmp receptors phosphorylate and activate smad1 directly. Phosphorylation of smad1 in vivo involves serines in the carboxy-terminal motif ssxs. These residues are phosphorylated directly by a bmp type i receptor in vitro |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
BMPR1A/1B/2 | up-regulates activity
phosphorylation
|
SMAD1 |
0.679 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217985 |
Ser463 |
SPHNPISsVS |
Homo sapiens |
|
| pmid |
sentence |
| 9136927 |
Here, we report that BMP receptors phosphorylate and activate Smad1 directly. Phosphorylation of Smad1 in vivo involves serines in the carboxy-terminal motif SSXS. These residues are phosphorylated directly by a BMP type I receptor in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217989 |
Ser465 |
HNPISSVs |
Homo sapiens |
|
| pmid |
sentence |
| 9136927 |
Here, we report that BMP receptors phosphorylate and activate Smad1 directly. Phosphorylation of Smad1 in vivo involves serines in the carboxy-terminal motif SSXS. These residues are phosphorylated directly by a BMP type I receptor in vitro |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Epithelium |
| + |
BMP7 | up-regulates
binding
|
BMPR1A/1B/2 |
0.788 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217520 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7644468 |
In transfected cos-1 cells, osteogenic protein (op)-1/bmp-7, and less efficiently bmp-4, bound to bmpr-ii. Bmpr-ii bound ligands only weakly alone, but the binding was facilitated by the presence of previously identified type i receptors for bmps. Binding of op-1/bmp-7 to bmpr-ii was also observed in nontransfected cell lines. Moreover, a transcriptional activation signal was transduced by bmpr-ii in the presence of type i receptors after stimulation by op-1/bmp-7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Adipogenesis |
| + |
NOTCH1 | up-regulates 
|
BMPR1A/1B/2 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-114592 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Similar synergy is found in notch and bmp crosstalk: activating notch signaling enhanced bmp-induced alp activity and formation of calcified nodules in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMP15 | up-regulates
binding
|
BMPR1A/1B/2 |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217538 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16446785 |
Here we have performed a detailed in situ hybridization analysis of the spatial and temporal expression patterns of the bmp ligands (bmp-2, -3, -3b, -4, -6, -7, -15), receptors (bmpr-ia, -ib, -ii), and bmp antagonist, follistatin, in rat ovaries over the normal estrous cycle. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Ovary |
| + |
BMP2 | up-regulates
binding
|
BMPR1A/1B/2 |
0.867 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217532 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7791754 |
Bmpr-ii is a transmembrane serine/threonine kinase that binds bmp-2 and bmp-7 in association with multiple type i receptors, including bmpr-ia/brk1, bmpr-ib, and actr-i, which is also an activin type i receptor. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-237000 |
|
|
Mus musculus |
MC3T3-E1 Cell |
| pmid |
sentence |
| 11714695 |
For this, bmp-2 binds first to the high affinity receptor bri and then recruits brii into the signaling complex. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| + |
BMP4 | up-regulates
binding
|
BMPR1A/1B/2 |
0.858 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217535 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7673243 |
We have isolated a cdna encoding a novel transmembrane serine/threonine kinase from human skin fibroblasts which we demonstrate here to be a type ii receptor that binds bmp-4. This receptor (brk-3) is distantly related to other known type ii receptors and is distinguished from them by an extremely long carboxyl-terminal sequence following the intracellular kinase domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skin |
| Pathways: | Adipogenesis |
| + |
NOG | down-regulates 
binding
|
BMPR1A/1B/2 |
0.618 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217529 |
|
|
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 bmpby blocking the molecular interfaces of the binding epitopes for both type i and type ii receptors |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217541 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12478285 |
Noggin binds the domain that is re-quired for bmp-7 to interact with bmp type i and type ii receptors.Noggin Inhibits bmpby blocking the molecular interfaces of the binding epitopes for both type i and type ii receptors |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
BMP4 | up-regulates activity
binding
|
BMPR1A/1B/2 |
0.858 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235376 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 11282024 |
Bmp-4 and gdf-5 are known to bind to activin |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236932 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8006002 |
BMP-4 bound to ALK-3 and ALK-6 efficiently |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| Pathways: | Adipogenesis |
| + |
GDF6 | up-regulates
binding
|
BMPR1A/1B/2 |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217526 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16049014 |
We found that transfection of small hairpin rna for bmprii and actriia in mc3t3 cells suppressed the signaling of gdf6, gdf7, and bmp10. Thus, the present approach provides a genomic paradigm for matching paralogous polypeptide ligands with a limited number of evolutionarily related receptors capable of activating specific downstream smad proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR2 | form complex 
binding
|
BMPR1A/1B/2 |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-33443 |
|
|
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 |
| + |
BMP7 | up-regulates activity
binding
|
BMPR1A/1B/2 |
0.788 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-232216 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7791754 |
BMPR-II is a transmembrane serine/threonine kinase that binds BMP-2 and BMP-7 in association with multiple type I receptors, including BMPR-IA/Brk1, BMPR-IB, and ActR-I, which is also an activin type I receptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Adipogenesis |
| + |
BMPR1A/1B/2 | up-regulates
phosphorylation
|
BMPR1A/1B/2 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217029 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18756288 |
Bmp ligands bind to the bmp receptors bmpr1 and bmpr2, and bmpr2 then phosphorylates and activates bmpr1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Adipogenesis |
| + |
BMPR1A | form complex
binding
|
BMPR1A/1B/2 |
0.58 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255257 |
|
|
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 |
| + |
BMPR1B | form complex
binding
|
BMPR1A/1B/2 |
0.577 |
| 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 |
| + |
NOTCH | up-regulates
|
BMPR1A/1B/2 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254335 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Similar synergy is found in notch and bmp crosstalk: activating notch signaling enhanced bmp-induced alp activity and formation of calcified nodules in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
BMPR1A/1B/2