| + |
P4HB | up-regulates quantity by stabilization 
binding
|
Collagen |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269731 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9545296 |
We also show that PDI associates independently with the C-propeptide of monomeric procollagen chains prior to trimer formation, indicating a role for this protein in coordinating the assembly of heterotrimeric molecules. This demonstrates that PDI has multiple functions in the folding of the same protein, that is, as a catalyst for disulfide bond formation, as a subunit of P4-H during proline hydroxylation, and independently as a molecular chaperone during chain assembly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Collagen | up-regulates 
|
ECM_synthesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269732 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 35268340 |
The extracellular matrix is a structure composed of many molecules, including fibrillar (types I, II, III, V, XI, XXIV, XXVII) and non-fibrillar collagens (mainly basement membrane collagens: types IV, VIII, X), non-collagenous glycoproteins (elastin, laminin, fibronectin, thrombospondin, tenascin, osteopontin, osteonectin, entactin, periostin) embedded in a gel of negatively charged water-retaining glycosaminoglycans (GAGs) such as non-sulfated hyaluronic acid (HA) and sulfated GAGs which are linked to a core protein to form proteoglycans (PGs). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
P4HA1 | up-regulates quantity
chemical modification
|
Collagen |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279877 |
|
|
Homo sapiens |
Pancreatic Ductal Adenocarcinoma Cell |
| pmid |
sentence |
| 40332386 |
P4HA1 Mediates Hypoxia-Induced Invasion in Human Pancreatic Cancer Organoids.Collagen prolyl 4-hydroxylase subunit alpha-1 (P4HA1) is the most common isoform of the collagen prolyl 4-hydroxylases and contributes to collagen synthesis and deposition |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
P4HA2 | up-regulates quantity by stabilization
hydroxylation
|
Collagen |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269733 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9211872 |
Prolyl 4-hydroxylase (proline hydroxylase, EC 1.14.11.2) catalyzes the hydroxylation of proline in -Xaa-Pro-Gly- triplets in collagens and other proteins with collagen-like sequences. The enzyme plays a central role in the synthesis of all collagens, as the 4-hydroxyproline residues formed in the reaction are essential for the folding of the newly synthesized collagen polypeptide chains into triple helical molecules. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
Collagen