RNF14

Protein-coding gene in the species Homo sapiens
RNF14
Identifiers
AliasesRNF14, ARA54, HFB30, TRIAD2, HRIHFB2038, ring finger protein 14
External IDsOMIM: 605675; MGI: 1929668; HomoloGene: 129170; GeneCards: RNF14; OMA:RNF14 - orthologs
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for RNF14
Genomic location for RNF14
Band5q31.3Start141,958,328 bp[1]
End141,990,292 bp[1]
Gene location (Mouse)
Chromosome 18 (mouse)
Chr.Chromosome 18 (mouse)[2]
Chromosome 18 (mouse)
Genomic location for RNF14
Genomic location for RNF14
Band18 B3|18 20.2 cMStart38,417,590 bp[2]
End38,450,902 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • endothelial cell

  • oocyte

  • secondary oocyte

  • right testis

  • right adrenal cortex

  • left testis

  • Achilles tendon

  • islet of Langerhans

  • rectum

  • left adrenal gland
Top expressed in
  • CA3 field

  • perirhinal cortex

  • entorhinal cortex

  • dorsal tegmental nucleus

  • central gray substance of midbrain

  • superior colliculus

  • subiculum

  • ventral tegmental area

  • inferior colliculus

  • medulla oblongata
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • ubiquitin protein ligase activity
  • transcription coactivator activity
  • metal ion binding
  • ubiquitin-protein transferase activity
  • ubiquitin-like protein transferase activity
  • protein binding
  • androgen receptor binding
  • ubiquitin conjugating enzyme binding
  • transferase activity
Cellular component
  • cytoplasm
  • ubiquitin ligase complex
  • nucleus
  • cytosol
Biological process
  • androgen receptor signaling pathway
  • regulation of transcription, DNA-templated
  • regulation of transcription by RNA polymerase II
  • protein polyubiquitination
  • transcription, DNA-templated
  • positive regulation of transcription, DNA-templated
  • protein ubiquitination
  • regulation of androgen receptor signaling pathway
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process
  • signal transduction
  • ubiquitin-dependent protein catabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9604

56736

Ensembl

ENSG00000013561

ENSMUSG00000060450

UniProt

Q9UBS8

Q9JI90

RefSeq (mRNA)
NM_001201365
NM_004290
NM_183398
NM_183399
NM_183400

NM_183401

NM_001164621
NM_001164622
NM_020012
NM_001361264
NM_001361265

NM_001361266
NM_001361267
NM_001361268
NM_001361269

RefSeq (protein)
NP_001188294
NP_004281
NP_899645
NP_899646
NP_899647

NP_899648

NP_001158093
NP_001158094
NP_064396
NP_001348193
NP_001348194

NP_001348195
NP_001348196
NP_001348197
NP_001348198

Location (UCSC)Chr 5: 141.96 – 141.99 MbChr 18: 38.42 – 38.45 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

E3 ubiquitin-protein ligase RNF14 is an enzyme that in humans is encoded by the RNF14 gene.[5][6][7]

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.[7] 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.[8]

Interactions

RNF14 has been shown to interact with the Androgen receptor.[5][9][10][11]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000013561 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000060450 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Kang HY, Yeh S, Fujimoto N, Chang C (Apr 1999). "Cloning and characterization of human prostate coactivator ARA54, a novel protein that associates with the androgen receptor". J Biol Chem. 274 (13): 8570–6. doi:10.1074/jbc.274.13.8570. PMID 10085091.
  6. ^ Ueki N, Seki N, Yano K, Masuho Y, Saito T, Muramatsu M (Jun 1999). "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. doi:10.1016/s0167-4781(99)00045-7. PMID 10320776.
  7. ^ a b EntrezGene 9604
  8. ^ Ingham AB, Osborne SA, Menzies M, Briscoe S, Chen W, Kongsuwan K, et al. (January 2014). "RNF14 is a regulator of mitochondrial and immune function in muscle". BMC Systems Biology. 8: 10. doi:10.1186/1752-0509-8-10. PMC 3906743. PMID 24472305.
  9. ^ Miyamoto H, Rahman M, Takatera H, Kang HY, Yeh S, Chang HC, Nishimura K, Fujimoto N, Chang C (Feb 2002). "A dominant-negative mutant of androgen receptor coregulator ARA54 inhibits androgen receptor-mediated prostate cancer growth". J. Biol. Chem. 277 (7): 4609–17. doi:10.1074/jbc.M108312200. PMID 11673464.
  10. ^ He B, Minges JT, Lee LW, Wilson EM (Mar 2002). "The FXXLF motif mediates androgen receptor-specific interactions with coregulators". J. Biol. Chem. 277 (12): 10226–35. doi:10.1074/jbc.M111975200. PMID 11779876.
  11. ^ He B, Wilson EM (Mar 2003). "Electrostatic modulation in steroid receptor recruitment of LXXLL and FXXLF motifs". Mol. Cell. Biol. 23 (6): 2135–50. doi:10.1128/mcb.23.6.2135-2150.2003. PMC 149467. PMID 12612084.

Further reading

  • Ueki N, Oda T, Kondo M, Yano K, Noguchi T, Muramatsu M (1999). "Selection system for genes encoding nuclear-targeted proteins". Nat. Biotechnol. 16 (13): 1338–42. doi:10.1038/4315. PMID 9853615. S2CID 20001769.
  • Ito K, Adachi S, Iwakami R, Yasuda H, Muto Y, Seki N, Okano Y (2001). "N-Terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8". Eur. J. Biochem. 268 (9): 2725–32. doi:10.1046/j.1432-1327.2001.02169.x. PMID 11322894.
  • Miyamoto H, Rahman M, Takatera H, Kang HY, Yeh S, Chang HC, Nishimura K, Fujimoto N, Chang C (2002). "A dominant-negative mutant of androgen receptor coregulator ARA54 inhibits androgen receptor-mediated prostate cancer growth". J. Biol. Chem. 277 (7): 4609–17. doi:10.1074/jbc.M108312200. PMID 11673464.
  • Ueda T, Mawji NR, Bruchovsky N, Sadar MD (2002). "Ligand-independent activation of the androgen receptor by interleukin-6 and the role of steroid receptor coactivator-1 in prostate cancer cells". J. Biol. Chem. 277 (41): 38087–94. doi:10.1074/jbc.M203313200. PMID 12163482.
  • He B, Wilson EM (2003). "Electrostatic Modulation in Steroid Receptor Recruitment of LXXLL and FXXLF Motifs". Mol. Cell. Biol. 23 (6): 2135–50. doi:10.1128/MCB.23.6.2135-2150.2003. PMC 149467. PMID 12612084.
  • Mestayer C, Blanchère M, Jaubert F, Dufour B, Mowszowicz I (2003). "Expression of androgen receptor coactivators in normal and cancer prostate tissues and cultured cell lines". Prostate. 56 (3): 192–200. doi:10.1002/pros.10229. PMID 12772188. S2CID 23253844.
  • Wang L, Hsu CL, Ni J, Wang PH, Yeh S, Keng P, Chang C (2004). "Human Checkpoint Protein hRad9 Functions as a Negative Coregulator To Repress Androgen Receptor Transactivation in Prostate Cancer Cells". Mol. Cell. Biol. 24 (5): 2202–13. doi:10.1128/MCB.24.5.2202-2213.2004. PMC 350564. PMID 14966297.
  • Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
  • Lin DY, Fang HI, Ma AH, Huang YS, Pu YS, Jenster G, Kung HJ, Shih HM (2004). "Negative Modulation of Androgen Receptor Transcriptional Activity by Daxx". Mol. Cell. Biol. 24 (24): 10529–41. doi:10.1128/MCB.24.24.10529-10541.2004. PMC 533990. PMID 15572661.
  • Yang Z, Chang YJ, Miyamoto H, Ni J, Niu Y, Chen Z, Chen YL, Yao JL, di Sant'Agnese PA, Chang C (2007). "Transgelin functions as a suppressor via inhibition of ARA54-enhanced androgen receptor transactivation and prostate cancer cell growth". Mol. Endocrinol. 21 (2): 343–58. doi:10.1210/me.2006-0104. PMID 17082327.
  • Yang Z, Chang YJ, Miyamoto H, Yeh S, Yao JL, di Sant'Agnese PA, Tsai MY, Chang C (2007). "Suppression of androgen receptor transactivation and prostate cancer cell growth by heterogeneous nuclear ribonucleoprotein A1 via interaction with androgen receptor coregulator ARA54". Endocrinology. 148 (3): 1340–9. doi:10.1210/en.2006-0716. PMID 17110431.
  • Kikuchi H, Uchida C, Hattori T, Isobe T, Hiramatsu Y, Kitagawa K, Oda T, Konno H, Kitagawa M (2007). "ARA54 is involved in transcriptional regulation of the cyclin D1 gene in human cancer cells". Carcinogenesis. 28 (8): 1752–8. doi:10.1093/carcin/bgm120. PMID 17510080.

External links

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

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Coactivators
Corepressors
ATP-dependent remodeling factors
  • Chromatin Structure Remodeling (RSC) Complex
  • SWI/SNF


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