P4HB

P4HB
Prolyl 4-hydroxylase, beta polypeptide

PDB rendering based on 1bjx.
Identifiers
Symbols P4HB; DSI; ERBA2L; GIT; P4Hbeta; PDI; PDIA1; PHDB; PO4DB; PO4HB; PROHB
External IDs OMIM176790 MGI97464 HomoloGene55495 GeneCards: P4HB Gene
EC number 5.3.4.1
RNA expression pattern
PBB GE P4HB 200656 s at tn.png
PBB GE P4HB 200654 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5034 18453
Ensembl ENSG00000185624 ENSMUSG00000025130
UniProt P07237 Q3TF72
RefSeq (mRNA) NM_000918 NM_011032.2
RefSeq (protein) NP_000909 NP_035162.1
Location (UCSC) Chr 17:
79.8 – 79.82 Mb
Chr 11:
120.42 – 120.43 Mb
PubMed search [1] [2]

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

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,[3] ERO1LB[4][5] and ERO1L.[4][5]

References

  1. ^ Shoulders CC, Brett DJ, Bayliss JD, Narcisi TM, Jarmuz A, Grantham TT, Leoni PR, Bhattacharya S, Pease RJ, Cullen PM, et al. (Mar 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. 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". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5034. 
  3. ^ Ko, Han Seok; Uehara Takashi, Nomura Yasuyuki (Sep. 2002). "Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death". J. Biol. Chem. (United States) 277 (38): 35386–92. doi:10.1074/jbc.M203412200. ISSN 0021-9258. PMID 12095988. 
  4. ^ a b Anelli, Tiziana; Alessio Massimo, Mezghrani Alexandre, Simmen Thomas, Talamo Fabio, Bachi Angela, Sitia Roberto (Feb. 2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". EMBO J. (England) 21 (4): 835–44. doi:10.1093/emboj/21.4.835. ISSN 0261-4189. PMC 125352. PMID 11847130. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125352. 
  5. ^ 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". EMBO J. (England) 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. ISSN 0261-4189. PMC 125306. PMID 11707400. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125306. 

Further reading


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