| + |
CTSD | down-regulates quantity by destabilization 
cleavage
|
BGLAP |
0.319 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256319 |
Ala92 |
DHIGFQEaYRRFYGP |
in vitro |
|
| pmid |
sentence |
| 9076588 |
This study has been undertaken to compare the degradation of BGP by the cysteine proteinases cathepsins L, B, H, S, and the aspartic proteinase cathepsin D. Cathepsins B, L, H, and S readily cleave BGP at the G7-A8 bond; cathepsin L also cleaves at R43-R44; cathepsin B also cleaves at R44-F45; and cathepsin D cleaves only at A41-Y42. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CTSH | down-regulates quantity by destabilization
cleavage
|
BGLAP |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256325 |
Arg94 |
IGFQEAYrRFYGPV |
in vitro |
|
| pmid |
sentence |
| 9076588 |
This study has been undertaken to compare the degradation of BGP by the cysteine proteinases cathepsins L, B, H, S, and the aspartic proteinase cathepsin D. Cathepsins B, L, H, and S readily cleave BGP at the G7-A8 bond; cathepsin L also cleaves at R43-R44; cathepsin B also cleaves at R44-F45; and cathepsin D cleaves only at A41-Y42. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256324 |
Gly58 |
RYLYQWLgAPVPYPD |
in vitro |
|
| pmid |
sentence |
| 9076588 |
This study has been undertaken to compare the degradation of BGP by the cysteine proteinases cathepsins L, B, H, S, and the aspartic proteinase cathepsin D. Cathepsins B, L, H, and S readily cleave BGP at the G7-A8 bond; cathepsin L also cleaves at R43-R44; cathepsin B also cleaves at R44-F45; and cathepsin D cleaves only at A41-Y42. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CTSL | down-regulates quantity by destabilization
cleavage
|
BGLAP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256322 |
Arg94 |
IGFQEAYrRFYGPV |
in vitro |
|
| pmid |
sentence |
| 9076588 |
This study has been undertaken to compare the degradation of BGP by the cysteine proteinases cathepsins L, B, H, S, and the aspartic proteinase cathepsin D. Cathepsins B, L, H, and S readily cleave BGP at the G7-A8 bond; cathepsin L also cleaves at R43-R44; cathepsin B also cleaves at R44-F45; and cathepsin D cleaves only at A41-Y42. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256321 |
Gly58 |
RYLYQWLgAPVPYPD |
in vitro |
|
| pmid |
sentence |
| 9076588 |
This study has been undertaken to compare the degradation of BGP by the cysteine proteinases cathepsins L, B, H, S, and the aspartic proteinase cathepsin D. Cathepsins B, L, H, and S readily cleave BGP at the G7-A8 bond; cathepsin L also cleaves at R43-R44; cathepsin B also cleaves at R44-F45; and cathepsin D cleaves only at A41-Y42. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CTSB | down-regulates quantity by destabilization
cleavage
|
BGLAP |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256320 |
Arg95 |
GFQEAYRrFYGPV |
in vitro |
|
| pmid |
sentence |
| 9076588 |
This study has been undertaken to compare the degradation of BGP by the cysteine proteinases cathepsins L, B, H, S, and the aspartic proteinase cathepsin D. Cathepsins B, L, H, and S readily cleave BGP at the G7-A8 bond; cathepsin L also cleaves at R43-R44; cathepsin B also cleaves at R44-F45; and cathepsin D cleaves only at A41-Y42. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256318 |
Gly58 |
RYLYQWLgAPVPYPD |
in vitro |
|
| pmid |
sentence |
| 9076588 |
This study has been undertaken to compare the degradation of BGP by the cysteine proteinases cathepsins L, B, H, S, and the aspartic proteinase cathepsin D. Cathepsins B, L, H, and S readily cleave BGP at the G7-A8 bond; cathepsin L also cleaves at R43-R44; cathepsin B also cleaves at R44-F45; and cathepsin D cleaves only at A41-Y42. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CTSS | down-regulates quantity by destabilization
cleavage
|
BGLAP |
0.314 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256323 |
Gly58 |
RYLYQWLgAPVPYPD |
in vitro |
|
| pmid |
sentence |
| 9076588 |
This study has been undertaken to compare the degradation of BGP by the cysteine proteinases cathepsins L, B, H, S, and the aspartic proteinase cathepsin D. Cathepsins B, L, H, and S readily cleave BGP at the G7-A8 bond; cathepsin L also cleaves at R43-R44; cathepsin B also cleaves at R44-F45; and cathepsin D cleaves only at A41-Y42. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SP7 | up-regulates quantity by expression 
transcriptional regulation
|
BGLAP |
0.515 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255409 |
|
|
Mus musculus |
C3H10T1/2 Cell, C2C12 Cell |
| pmid |
sentence |
| 11792318 |
To test whether Osx could activate typical osteoblast genes, we transfected an Osx expressing vector into both C2C12 and C3H10T1/2 cells. Our results showed that Osx produced an induction of osteocalcin RNA in both cell types. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ETS2 | up-regulates quantity by expression 
transcriptional regulation
|
BGLAP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259875 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 11175361 |
Ets2 is expressed at high levels during the differentiation and matrix mineralization phases of MC3T3-E1 culture. In addition, several extracellular matrix (ECM) associated gene products are targets of Ets2. Some of these matrix associated genes include: bone sialoprotein, osteonectin, osteocalcin and osteopontin |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
GGCX | up-regulates activity
carboxylation
|
BGLAP |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265922 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31226734 |
Thus, vitamin K acts as a cofactor for GGCX via the vitamin K cycle and exerts physiological effects through its regulation of VKDPs [29]. More than 20 VKDPs have been found. Osteocalcin promotes bone formation, and blood coagulation factors II, VII, IX, and X activate blood coagulation. Matrix Gla protein suppresses cardiovascular calcification, and brain-expressed Gas 6 promotes neural differentiation [29]. GGCX is an enzyme that converts glutamic acid (Glu) residues to Gla residues, so that the Gla-containing proteins can exert various physiological actions such as blood coagulation and bone formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Vitamin-K cycle |
| + |
SMOC1 | up-regulates quantity by expression
transcriptional regulation
|
BGLAP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260400 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20359165 |
The expression of several osteoblast differentiation markers (ALP, COL1, OPN, ON, BSP and OC) was higher in SMOC1-overexpressing cells than in emptyvector-expressing cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TGFB1 | down-regulates quantity by repression 
transcriptional regulation
|
BGLAP |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107248 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11331591 |
Tgf-beta inhibited the expression of the cbfa1 and_ osteocalcin_ genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUNX2 | up-regulates quantity by expression
transcriptional regulation
|
BGLAP |
0.603 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107160 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11331591 |
Tgf-beta inhibited the expression of the cbfa1 and osteocalcin genes, whose expression is controlled by cbfa1 in osteoblast-like cell lines. This inhibition was mediated by smad3, which interacts physically with cbfa1 and represses its transcriptional activity at the cbfa1-binding ose2 promoter sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255408 |
|
|
Mus musculus |
F9-12 Cell, ROS-17/2.8 Cell |
| pmid |
sentence |
| 9182762 |
Indeed, we identified Osf2/Cbfa1 binding sites in the promoter of four genes expressed only (the Osteocalcin genes) or highly (α1(I) collagen, Bsp, and Osteopontin) in osteoblasts. Each of these elements was able to bind Osf2/Cbfa1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| + |
RUNX2/EP300 | up-regulates quantity by expression
transcriptional regulation
|
BGLAP |
0.439 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255420 |
|
|
Rattus norvegicus |
ROS-17/2.8 Cell |
| pmid |
sentence |
| 12697832 |
In agreement with our studies in ROS 17/2.8 cells, coexpression of p300 and Runx2/Cbfa1 resulted in marked enhancement of the OC promoter activity, further indicating that both factors cooperate to stimulate this promoter. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
3.0
BGLAP
- 
- 