HIF1A

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Hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor), also known as HIF1A, is a human gene.

Hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
PDB rendering based on 1h2k.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols HIF1A ; HIF-1alpha; HIF1-ALPHA; MOP1; PASD8
External IDs Template:OMIM5 Template:MGI HomoloGene1171
RNA expression pattern
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

The protein encoded by HIF1 is a transcription factor found in mammalian cells growing at low oxygen concentrations. It plays an essential role in cellular and systemic responses to hypoxia.[1] This is one of the class of hypoxia inducible factors.

HIF1 is a heterodimer composed of an alpha subunit and a beta subunit. The beta subunit has been identified as the aryl hydrocarbon receptor nuclear translocator (ARNT). This gene encodes the alpha subunit of HIF-1. Overexpression of a natural antisense transcript (aHIF) of this gene is associated with nonpapillary renal carcinomas.[2] Two alternative transcripts encoding different isoforms have been identified.[3]


References

  1. Ratcliffe PJ (2003). "From erythropoietin to oxygen: hypoxia-inducible factor hydroxylases and the hypoxia signal pathway". Blood Purif. 20 (5): 445–50. PMID 12207089.
  2. Quintero M, Mackenzie N, Brennan PA (2004). "Hypoxia-inducible factor 1 (HIF-1) in cancer". Eur J Surg Oncol. 30 (5): 465–8. doi:10.1016/j.ejso.2004.03.008. PMID 15135470.
  3. "Entrez Gene: HIF1A hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)".

Further reading

  • Semenza GL (2000). "HIF-1 and human disease: one highly involved factor". Genes Dev. 14 (16): 1983–91. PMID 10950862.
  • Semenza G (2002). "Signal transduction to hypoxia-inducible factor 1". Biochem. Pharmacol. 64 (5–6): 993–8. PMID 12213597.
  • Arbeit JM (2003). "Quiescent hypervascularity mediated by gain of HIF-1 alpha function". Cold Spring Harb. Symp. Quant. Biol. 67: 133–42. PMID 12858534.
  • Sitkovsky M, Lukashev D (2005). "Regulation of immune cells by local-tissue oxygen tension: HIF1 alpha and adenosine receptors". Nat. Rev. Immunol. 5 (9): 712–21. doi:10.1038/nri1685. PMID 16110315.
  • Mobasheri A, Richardson S, Mobasheri R; et al. (2006). "Hypoxia inducible factor-1 and facilitative glucose transporters GLUT1 and GLUT3: putative molecular components of the oxygen and glucose sensing apparatus in articular chondrocytes". Histol. Histopathol. 20 (4): 1327–38. PMID 16136514.
  • Schipani E (2006). "Hypoxia and HIF-1 alpha in chondrogenesis". Semin. Cell Dev. Biol. 16 (4–5): 539–46. doi:10.1016/j.semcdb.2005.03.003. PMID 16144691.
  • Haase VH (2006). "Hypoxia-inducible factors in the kidney". Am. J. Physiol. Renal Physiol. 291 (2): F271–81. doi:10.1152/ajprenal.00071.2006. PMID 16554418.
  • Liang D, Kong X, Sang N (2007). "Effects of histone deacetylase inhibitors on HIF-1". Cell Cycle. 5 (21): 2430–5. PMID 17102633.


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