EC Number   |
General Information |
Reference  |
|---|
   1.14.11.7 | malfunction |
epigenetic inactivation of the enzyme in human cancer |
697017 |
| 1.14.11.7 | physiological function |
the enzyme acts as a tumor suppressor |
697017 |
| 1.14.11.7 | physiological function |
the enzyme acts as a tumor suppressor, with P3H2 being a specific breast-cancer tumour suppressor |
697017 |
| 1.14.11.7 | malfunction |
in case of enzyme defects, 3-hydroxylation of the Pro986 residue is absent or severly reduced. Defects in the genes encoding cartilage-associated protein, CRTAP, or prolyl 3-hydroxylase 1, P3H1/LEPRE1, cause the classical osteogenesis imperfecta, OI, a dominant genetic disorder of connective tissue, overview. Patients with mutations in CRTAP or LEPRE1 have a lethal to severe osteochondrodystrophy that overlaps with Sillence types II and III classical osteogenesis imperfecta but has distinctive features |
697192 |
| 1.14.11.7 | malfunction |
null mutation of the prolyl 3-hydroxylase 1, P3H1/LEPRE1, gene cause OI type VIII, a recessive form of osteogenesis imperfecta with severe to lethal bone dysplasia and overmodification of the type I collagen helical region, overview |
698181 |
| 1.14.11.7 | more |
PHD3 upregulation contributes to doxorubicin-induced apoptosis in H9c2 cells. Overexpression of PHD3 counteracts the formation of the BaxBcl-2 complex, the BH4 domain of anti-apoptosis protein Bcl-2 is required for its interaction with PHD3. BaxBcl-2 complex formation is significantly reduced in apoptotic H9c2 cells in which PHD3 is overexpressed compared to the apoptotic H9c2 cells with native PHD3 levels |
711115 |
| 1.14.11.7 | physiological function |
role of PHD3 in the apoptosis of cardiac myocytes. PHD3 promotes the apoptosis of H9c2 cells via an interaction with the BH4 domain of Bcl-2, it affects the formation of the BaxBcl-2 complex |
711115 |
| 1.14.11.7 | more |
importance of P3H1 to bone structure and development. Mutations in the gene encoding for prolyl 3-hydroxylase 1 can cause a severe, recessive form of osteogenesis imperfecta, a skeletal disorder, minimal 3-hydroxylation of key proline residues in type I collagen as a result of P3H1 deficiency. Prolyl 3-hydroxylase 1 null mice display abnormalities in fibrillar collagen-rich tissues such as tendons, skin, and bones, e.g. abnormalities in collagen fibril ultrastructure in tendons, and alterations in skin architecture, as well as in developing limbs, phenotypes, detailed overview. Collagen secretion rate is decreased in P3H1 null fibroblasts |
712433 |
| 1.14.11.7 | malfunction |
a knockdown of P3H2 protein using RNA interference reduces 3-hydroxylation at Pro-944, Pro-707, and the GPP repeat at the C-terminus of the triple helix but not at Pro-986 of the clade A pNalpha1(II) collagen chain. When P3H2 expression is turned off, 3-hydroxylation at residue Pro-944 in the alpha2(V) chain is lost, and 3Hyp occupancy at Pro-707 in alpha2(V) and alpha2(I) chains is significantly reduced |
727884 |
| 1.14.11.7 | malfunction |
loss-of function studies show that PHD3 serves as a co-activator of NF-kappaB signaling activity in NP cells. PHD3 interacts with, and co-localizes with, p65 |
727931 |
