Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Gros1, a potential growth suppressor on chromosome 1: its identity to basement membrane-associated proteoglycan, leprecan.
Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes.
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P3H1 is an ER-resident 2-oxoglutarate/iron-dependent dioxygenase with prolyl 3-hydroxylase activity on full-length procollagen, specifically interacts with denatured collagen, and exists in a tight complex with other ER-resident proteins.
Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta.
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Null LEPRE1 alleles abolish alpha1(I)Pro986 3-hydroxylation, cause overmodification and delayed/altered collagen secretion, and produce recessive OI; P3H1 is crucial for bone development and collagen helix formation.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Recessive osteogenesis imperfecta caused by LEPRE1 mutations: clinical documentation and identification of the splice form responsible for prolyl 3-hydroxylation.
Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex.
Defining the membrane proteome of NK cells.
Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding.
A novel mutation in LEPRE1 that eliminates only the KDEL ER- retrieval sequence causes non-lethal osteogenesis imperfecta.
Cellular stress due to impairment of collagen prolyl hydroxylation complex is rescued by the chaperone 4-phenylbutyrate.
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Primary fibroblasts from recessive OI patients (including P3H1/LEPRE1 deficiency) retain overmodified type I collagen, causing ER enlargement, protein aggregates, PERK-branch unfolded protein response activation and apoptosis; 4-phenylbutyrate (4-PBA) restores ER proteostasis and cell survival.
Clinical spectrum of rare bone fragility disorders and response to bisphosphonate treatment: a retrospective study.
Comprehensive proteomic characterization of stem cell-derived extracellular matrices.
Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
The structural basis for the collagen processing by human P3H1/CRTAP/PPIB ternary complex.
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Cryo-EM structures of the P3H1/CRTAP/PPIB (PCP) ternary and dual-ternary complexes, with 2-oxoglutarate and Fe, and with a collagen peptide; P3H1 is the core prolyl 3-hydroxylase hydroxylating Pro986 of collagen alpha1(I).
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P3H1 and PPIB active sites form a face-to-face bifunctional reaction center; active-site mutations (H587A, D589A, H659A, R669) abolish/severely reduce 2OG-dependent oxygenase activity, confirming the catalytic residues.
Collagen prolyl 3-hydroxylase converts 4-Hyp collagen to 3,4-Hyp collagen
Procollagen triple helix formation
Prolyl 3-hydroxylases:Fe2+:3,4-Hyp collagen propeptides dissociates
P3HB binds 4-Hyp-collagen propeptides
UniProt entry Q32P28 (P3H1_HUMAN), prolyl 3-hydroxylase 1