Jump to content

P4HB

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Boghog (talk | contribs) at 12:02, 28 December 2015 (Applications: removed spamy section). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

Template:PBB Protein disulfide-isomerase is an enzyme that in humans is encoded by the P4HB gene.[1][2][3]

Function

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.[2]

Interactions

P4HB has been shown to interact with UBQLN1,[4] ERO1LB[5][6] and ERO1L.[5][6]

References

  1. ^ Shoulders CC, Brett DJ, Bayliss JD, Narcisi TM, Jarmuz A, Grantham TT, Leoni PR, Bhattacharya S, Pease RJ, Cullen PM (Dec 1993). "Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein". Human Molecular Genetics. 2 (12): 2109–16. doi:10.1093/hmg/2.12.2109. PMID 8111381.
  2. ^ a b "Entrez Gene: P4HB procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide".
  3. ^ Galligan JJ, Petersen DR (July 2012). "The human protein disulfide isomerase gene family". Human Genomics. 6 (6): 6. doi:10.1186/1479-7364-6-6. PMC 3500226. PMID 23245351.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  4. ^ Ko HS, Uehara T, Nomura Y (Sep 2002). "Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death". The Journal of Biological Chemistry. 277 (38): 35386–92. doi:10.1074/jbc.M203412200. PMID 12095988.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  5. ^ a b Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R (Feb 2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". The EMBO Journal. 21 (4): 835–44. doi:10.1093/emboj/21.4.835. PMC 125352. PMID 11847130.
  6. ^ a b Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R (Nov 2001). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". The EMBO Journal. 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. PMC 125306. PMID 11707400.

Further reading