Biology:RNF14

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

E3 ubiquitin-protein ligase RNF14 is an enzyme that in humans is encoded by the RNF14 gene.[1][2][3]

Function

The protein encoded by this gene contains a RING zinc finger, a motif known to be involved in protein-protein interactions. This protein interacts with androgen receptor (AR) and may function as a coactivator that induces AR target gene expression in prostate. A dominant negative mutant of this gene has been demonstrated to inhibit the AR-mediated growth of prostate cancer. This protein also interacts with class III ubiquitin-conjugating enzymes (E2s) and may act as a ubiquitin-ligase (E3) in the ubiquitination of certain nuclear proteins. Five alternatively spliced transcript variants encoding two distinct isoforms have been reported.[3] Another function of RNF14 protein relates to its regulation of the inter-relationship between bioenergetic status and inflammation. It influences the expression of mitochondrial and immune-related genes in skeletal muscle including cytokines and interferon regulatory factors.[4]

Interactions

RNF14 has been shown to interact with the Androgen receptor.[1][5][6][7]

See also

References

  1. 1.0 1.1 "Cloning and characterization of human prostate coactivator ARA54, a novel protein that associates with the androgen receptor". J Biol Chem 274 (13): 8570–6. Apr 1999. doi:10.1074/jbc.274.13.8570. PMID 10085091. 
  2. "Isolation and characterization of a novel human gene (HFB30) which encodes a protein with a RING finger motif". Biochim Biophys Acta 1445 (2): 232–6. Jun 1999. doi:10.1016/s0167-4781(99)00045-7. PMID 10320776. 
  3. 3.0 3.1 EntrezGene 9604
  4. "RNF14 is a regulator of mitochondrial and immune function in muscle". BMC Systems Biology 8: 10. January 2014. doi:10.1186/1752-0509-8-10. PMID 24472305. 
  5. "A dominant-negative mutant of androgen receptor coregulator ARA54 inhibits androgen receptor-mediated prostate cancer growth". J. Biol. Chem. 277 (7): 4609–17. Feb 2002. doi:10.1074/jbc.M108312200. PMID 11673464. 
  6. "The FXXLF motif mediates androgen receptor-specific interactions with coregulators". J. Biol. Chem. 277 (12): 10226–35. Mar 2002. doi:10.1074/jbc.M111975200. PMID 11779876. 
  7. "Electrostatic modulation in steroid receptor recruitment of LXXLL and FXXLF motifs". Mol. Cell. Biol. 23 (6): 2135–50. Mar 2003. doi:10.1128/mcb.23.6.2135-2150.2003. PMID 12612084. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.