| + |
BMP1 | up-regulates quantity 
cleavage
|
COL7A1 |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256338 |
Ala2821 |
RPLPSYAaDTAGSQL |
Homo sapiens |
Keratinocyte |
| pmid |
sentence |
| 11986329 |
We show that bone morphogenetic protein-1 (BMP-1), which exhibits procollagen C-proteinase activity, cleaves the C-terminal propeptide from human procollagen VII. The cleavage occurs at the BMP-1 consensus cleavage site SYAA/DTAG within the NC-2 domain. Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMP1 | up-regulates activity
cleavage
|
COL5A1 |
0.607 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256344 |
Asp1549 |
IKTEEISeVKMDAEF |
Homo sapiens |
HEK-293-EBNA Cell |
| pmid |
sentence |
| 11741999 |
BMP-1 Can Efficiently Cleave Pro-α1(V) N-propeptides and Pro-α2(V) C-propeptides and Less Efficiently Cleave Pro-α1(V) C-propeptides in Vitro.NH2-terminal sequencing of an ∼35-kDa band in the BMP-1-treated material (N-α1(V), Fig. 3 B,lanes 2 and 3) showed it to correspond to the NH2-terminal portion of the pro-α1(V) N-propeptide previously shown to be cleaved in pro-α1(V)3 homotrimers by BMP-1 (39), whereas NH2-terminal sequencing of an ∼38-kDa band (C-α1(V)BMP-1, Fig. 3 B,lanes 2 and 3) showed it to correspond to pro-α1(V) C-propeptides cleaved between Asp-1594 and Asp-1595. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMP1 | up-regulates activity
cleavage
|
COL5A2 |
0.59 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256343 |
Glu1253 |
SEVKMDAeFRHDSGY |
Homo sapiens |
HEK-293-EBNA Cell |
| pmid |
sentence |
| 11741999 |
BMP-1 Can Efficiently Cleave Pro-α1(V) N-propeptides and Pro-α2(V) C-propeptides and Less Efficiently Cleave Pro-α1(V) C-propeptides in Vitro. BMP-1 efficiently cleaves pro-α2(V) C-propeptides at a single site between residues 1250 (Glu) and 1251 (Asp). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMP1 | up-regulates activity
cleavage
|
COL1A1 |
0.668 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256342 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11283002 |
BMP-1myc Expressed in COS-7 Cells Exhibits Procollagen C-proteinase Activity. Bone morphogenetic protein (BMP)-1, which belongs to the tolloid subgroup of astacin-like zinc metalloproteinases, cleaves the C-propeptides of procollagen at the physiologic site and is, therefore, a procollagen C-proteinase (PCP). Cleavage occurs between a specific alanine or glycine residue (depending on the procollagen chain) and an invariant aspartic acid residue in each of the three chains of procollagen. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
3.0
BMP1
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