P3H2 (Prolyl 3-Hydroxylase 2)
A key enzyme in collagen prolyl hydroxylation, essential for proper collagen folding and extracellular matrix integrity.
Gene Information Card
| Symbol | P3H2 |
|---|---|
| Full Name | Prolyl 3-Hydroxylase 2 |
| Gene Type | Protein coding |
| Chromosomal Location | 3q28 |
| NCBI Gene ID | 7157 ncbi.nlm.nih.gov/gene/7157 |
| Ensembl ID | ENSG00000163947 |
| UniProt ID | Q8IVL6 |
| OMIM ID | 610341 |
| HGNC ID | 19317 |
| Aliases | LPH3, LEPREL1, P3H2 |
Description
P3H2 encodes prolyl 3-hydroxylase 2, an enzyme that catalyzes the 3-hydroxylation of proline residues in collagen chains. This modification is critical for proper collagen triple helix formation, stability, and extracellular matrix assembly. The protein is localized to the endoplasmic reticulum and is highly expressed in tissues with abundant collagen, such as bone, skin, and tendons.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Osteogenesis Imperfecta Type XXIV | Loss-of-function mutations in P3H2 impair collagen 3-hydroxylation, leading to brittle bones and skeletal deformities. | ClinVar, OMIM |
| High Myopia | Missense variants in P3H2 have been associated with severe myopia, possibly due to altered scleral collagen structure. | ClinVar, PubMed |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Bone | 12.5 | High |
| Skin | 8.3 | Medium |
| Lung | 6.1 | Medium |
| Heart | 4.2 | Low |
| Liver | 1.8 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| Osteoblasts | 15.2 | High expression in bone-forming cells |
| Fibroblasts | 9.7 | Consistent with collagen synthesis |
| Chondrocytes | 7.4 | Cartilage matrix production |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.1072C>T (p.Arg358Trp) | Missense | <0.01% | Reduced enzyme activity; associated with high myopia |
| c.1A>G (p.Met1Val) | Start loss | Rare | Loss of protein expression; osteogenesis imperfecta |
| c.1543G>A (p.Gly515Arg) | Missense | <0.001% | Impaired collagen binding; skeletal dysplasia |
Mutation functional classification
Loss of Function (LOF)
Most pathogenic mutations in P3H2 are loss-of-function, leading to reduced 3-hydroxylation of collagen proline residues and compromised extracellular matrix integrity.
Gain of Function (GOF)
No gain-of-function mutations have been reported for P3H2.
Dominant Negative (DN)
No dominant-negative mechanisms are currently described for P3H2.
View complete mutation data：
Gene Ontology (GO)
| • prolyl 3-hydroxylase activity | • collagen binding |
| • endoplasmic reticulum lumen | • peptidyl-proline hydroxylation |
| • extracellular matrix organization |
Pathways
• Collagen biosynthesis and modifying enzymes
• Endoplasmic reticulum protein processing
Protein Summary
Prolyl 3-hydroxylase 2 is a 708-amino acid protein that resides in the endoplasmic reticulum. It forms a complex with cartilage-associated protein (CRTAP) and prolyl 3-hydroxylase 1 (P3H1) to hydroxylate specific proline residues in collagen alpha chains. This modification is essential for proper collagen folding and secretion. Mutations in P3H2 disrupt collagen maturation, leading to connective tissue disorders.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| P3H2 Knockout HEK293 Cell Line | EDJ-KQ14655 | Human | 55214 | Details Get a Quote |
| P3H2 Knockout A-549 Cell Line | EDJ-KQ44935 | Human | 55214 | Details Get a Quote |
| P3H2 Knockout HCT 116 Cell Line | EDJ-KQ44936 | Human | 55214 | Details Get a Quote |
| P3H2 Knockout HeLa Cell Line | EDJ-KQ44937 | Human | 55214 | Details Get a Quote |
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