Relation Results

Summary

Name Collagen
Primary ID SIGNOR-PF103
Type protein family
Formed by COL10A1, COL11A1, COL11A2, COL12A1, COL13A1, COL14A1, COL15A1, COL16A1, COL17A1, COL18A1, COL19A1, COL1A1, COL1A2, COL20A1, COL21A1, COL22A1, COL23A1, COL24A1, COL25A1, COL26A1, COL27A1, COL28A1, COL2A1, COL3A1, COL4A1, COL4A2, COL4A3, COL4A4, COL4A5, COL4A6, COL5A1, COL5A2, COL5A3, COL6A1, COL6A2, COL6A3, COL6A5, COL6A6, COL7A1, COL8A1, COL8A2, COL9A1, COL9A2, COL9A3
Relations 3

Viewer

Type: Score: Layout: SPV 
0.20.20.7P4HA2CollagenP4HBECM_synthesis

Search Tools

Refine search:

  • by mechanism


  • by effect
  • by organism:


  • by tissue:


  • by cell-line

Relations
Regulator
Mechanism
target
score ℹ
+ P4HA2up-regulates quantity by stabilization img/direct-activation.png hydroxylation Collagen 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-269733 Homo sapiens
pmid sentence
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
+ P4HBup-regulates quantity by stabilization img/direct-activation.png binding Collagen 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-269731 Homo sapiens
pmid sentence
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
+ Collagenup-regulates img/indirect-activation.png ECM_synthesis 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-269732 Homo sapiens
pmid sentence
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
a simple tooltip