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Literature summary for 1.14.11.7 extracted from

  • Chang, W.; Barnes, A.M.; Cabral, W.A.; Bodurtha, J.N.; Marini, J.C.
    Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex (2009), Hum. Mol. Genet., 19, 223-234.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.7

Protein Variants

Protein Variants Comment Organism
additional information 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, interaction of complex components in fibroblasts, overview. P3H1 is mutually stabilized in the collagen prolyl 3-hydroxylation complex. Both P3H1 and CRTAP proteins are absent in CRTAP-null fibroblasts. Conversely, in LEPRE1-null fibroblasts, P3H1 protein is absent, while CRTAP is only minimally detectable Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum collagen 3-hydroxylase complex Homo sapiens 5783
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q32P28 gene LEPRE1
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
LEPRE1
-
 Homo sapiens
P3H1
-
 Homo sapiens
prolyl 3-hydroxylase 1
-
 Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens