HIF1A

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: 1h2k, 1h2l, 1h2m, 1l3e, 1l8c, 1lqb
Identifiers
Symbol(s)	HIF1A; HIF-1alpha; HIF1-ALPHA; MOP1; PASD8
External IDs	OMIM: 603348 MGI: 106918 Homologene: 1171
Gene ontology Molecular Function: • RNA polymerase II transcription factor activity, enhancer binding • signal transducer activity • protein binding • histone acetyltransferase binding • protein heterodimerization activity Cellular Component: • nucleus • microtubule-based flagellum Biological Process: • angiogenesis • response to hypoxia • neural crest cell migration • heart looping • regulation of transcription, DNA-dependent • signal transduction • cell differentiation • homeostatic process • regulation of apoptosis • positive regulation of transcription • positive regulation of transcription from RNA polymerase II promoter
RNA expression pattern
More reference expression data
Orthologs
	Human	Mouse
Entrez	3091	15251
Ensembl	ENSG00000100644	ENSMUSG00000021109
Uniprot	Q16665	Q3UCW2
Refseq	NM_001530 (mRNA) NP_001521 (protein)	NM_010431 (mRNA) NP_034561 (protein)
Location	Chr 14: 61.23 - 61.28 Mb	Chr 12: 74.83 - 74.87 Mb
Pubmed search	[1]	[2]

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. 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. Two alternative transcripts encoding different isoforms have been identified.

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.