P4HB

Procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide
File:PBB Protein P4HB image.jpg PDB rendering based on 1bjx.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1bjx​, 1mek​, 1x5c​, 2bjx​
Identifiers
Symbols	P4HB ; DSI; ERBA2L; GIT; PDI; PDIA1; PHDB; PO4DB; PO4HB; PROHB
External IDs	Template:OMIM5 Template:MGI HomoloGene: 55495
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE P4HB 200656 s at tn.png
File:PBB GE P4HB 200654 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide, also known as P4HB, is a human gene.

This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex.

Further reading

• Pihlajaniemi T, Myllylä R, Kivirikko KI (1992). "Prolyl 4-hydroxylase and its role in collagen synthesis". J. Hepatol. 13 Suppl 3: S2–7. PMID 1667665.CS1 maint: Multiple names: authors list (link)
• Wilkinson B, Gilbert HF (2004). "Protein disulfide isomerase". Biochim. Biophys. Acta. 1699 (1–2): 35–44. doi:10.1016/j.bbapap.2004.02.017. PMID 15158710.
• Hochstrasser DF, Frutiger S, Paquet N; et al. (1993). "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis. 13 (12): 992–1001. PMID 1286669.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Chessler SD, Byers PH (1992). "Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern". J. Biol. Chem. 267 (11): 7751–7. PMID 1339453.
• Vuori K, Myllylä R, Pihlajaniemi T, Kivirikko KI (1992). "Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity". J. Biol. Chem. 267 (11): 7211–4. PMID 1559965.CS1 maint: Multiple names: authors list (link)
• Tasanen K, Oikarinen J, Kivirikko KI, Pihlajaniemi T (1992). "Promoter of the gene for the multifunctional protein disulfide isomerase polypeptide. Functional significance of the six CCAAT boxes and other promoter elements". J. Biol. Chem. 267 (16): 11513–9. PMID 1597478.CS1 maint: Multiple names: authors list (link)
• Bauw G, Rasmussen HH, van den Bulcke M; et al. (1990). "Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes". Electrophoresis. 11 (7): 528–36. doi:10.1002/elps.1150110703. PMID 1699755.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ward LD, Hong J, Whitehead RH, Simpson RJ (1991). "Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis". Electrophoresis. 11 (10): 883–91. doi:10.1002/elps.1150111019. PMID 2079031.CS1 maint: Multiple names: authors list (link)
• Tasanen K, Parkkonen T, Chow LT; et al. (1988). "Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase". J. Biol. Chem. 263 (31): 16218–24. PMID 2846539.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Koivu J, Myllylä R, Helaakoski T; et al. (1987). "A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase". J. Biol. Chem. 262 (14): 6447–9. PMID 3032969.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Pihlajaniemi T, Helaakoski T, Tasanen K; et al. (1987). "Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene". EMBO J. 6 (3): 643–9. PMID 3034602.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Morris JI, Varandani PT (1988). "Characterization of a cDNA for human glutathione-insulin transhydrogenase (protein-disulfide isomerase/oxidoreductase)". Biochim. Biophys. Acta. 949 (2): 169–80. PMID 3342239.
• Gosden JR, Middleton PG, Rout D, De Angelis C (1987). "Chromosomal localization of the human oncogene ERBA2". Cytogenet. Cell Genet. 43 (3–4): 150–3. PMID 3467900.CS1 maint: Multiple names: authors list (link)
• Cheng SY, Gong QH, Parkison C; et al. (1987). "The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum". J. Biol. Chem. 262 (23): 11221–7. PMID 3611107.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Helaakoski T, Annunen P, Vuori K; et al. (1995). "Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit". Proc. Natl. Acad. Sci. U.S.A. 92 (10): 4427–31. PMID 7753822.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Shoulders CC, Brett DJ, Bayliss JD; et al. (1994). "Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein". Hum. Mol. Genet. 2 (12): 2109–16. PMID 8111381.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kemmink J, Darby NJ, Dijkstra K; et al. (1996). "Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase". Protein Sci. 4 (12): 2587–93. PMID 8580850.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kemmink J, Darby NJ, Dijkstra K; et al. (1996). "Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy". Biochemistry. 35 (24): 7684–91. doi:10.1021/bi960335m. PMID 8672469.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ji H, Reid GE, Moritz RL; et al. (1997). "A two-dimensional gel database of human colon carcinoma proteins". Electrophoresis. 18 (3–4): 605–13. doi:10.1002/elps.1150180344. PMID 9150948.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)