P4HB

Chr 17q25.3

prolyl 4-hydroxylase subunit beta

Aliases:: PDIA1, PROHB, DSI, GIT, PDI
MANE:: ENST00000331483.9

OMIM: 176790 ↗NCBI: 5034 ↗Ensembl ↗

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Predicted protein structure

AlphaFold predicted structure

P4HB · P07237

v62025-08-01

Predicted Aligned Error matrix for P4HB — diagonal shows residue index, colour shows pairwise prediction confidence (lower is better) — Predicted Aligned Error

Mean pLDDT

88.5/ 100

Confident

508 residues

Confidence breakdown

Very high(≥ 90)71%
Confident(70–90)20%
Low(50–70)1%
Very low(< 50)9%

Open interactive 3D viewer

AlphaFold (Jumper et al., 2021) · CC BY 4.0

Clinical relevance (Genomics England PanelApp)

Diagnostic Grade (Green)

DDG2P
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknown
Fetal anomalies
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknown
Osteogenesis imperfecta
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Rare syndromic craniosynostosis or isolated multisuture synostosis
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Skeletal dysplasia
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Hydrocephalus
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknown
Intellectual disability
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted

Disease associations (Open Targets)

Cole-Carpenter syndrome
0.74
Hypercholesterolemia
0.53
familial hypercholesterolemia
0.52
dengue disease
0.47
cardiovascular disorder
0.38
osteogenesis imperfecta type 1
0.37
homozygous familial hypercholesterolemia
0.32
hereditary disease
0.19
osteogenesis imperfecta
0.13
breast cancer
0.11

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

Protein disulfide-isomerase

This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins (PubMed:32149426). At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307)