HIF1A information

HIF1A
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1H2K, 1H2L, 1H2M, 1L3E, 1L8C, 1LM8, 1LQB, 2ILM, 3HQR, 3HQU, 4AJY, 4H6J
Identifiers
Aliases	HIF1A, HIF-1-alpha, HIF-1A, HIF-1alpha, HIF1, HIF1-ALPHA, MOP1, PASD8, bHLHe78, hypoxia inducible factor 1 alpha subunit, hypoxia inducible factor 1 subunit alpha, HIF-1α
External IDs	OMIM: 603348; MGI: 106918; HomoloGene: 1171; GeneCards: HIF1A; OMA:HIF1A - orthologs
Gene location (Human)
Chr.	Chromosome 14 (human)
End	61,748,259 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	73,994,304 bp
RNA expression pattern
	Top expressed in
	pancreatic ductal cell; ; corpus epididymis; ; caput epididymis; ; tibia; ; cartilage tissue; ; gingival epithelium; ; visceral pleura; ; tail of epididymis; ; seminal vesicula; ; epithelium of nasopharynx;
	Top expressed in
	pineal gland; ; retina; ; stria vascularis; ; cumulus cell; ; epithelium of lens; ; iris; ; Gonadal ridge; ; calvaria; ; abdominal wall; ; vestibular sensory epithelium;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein dimerization activity; DNA-binding transcription factor activity; DNA-binding transcription activator activity, RNA polymerase II-specific; histone deacetylase binding; transcription factor binding; enzyme binding; protein binding; histone acetyltransferase binding; protein kinase binding; Hsp90 protein binding; sequence-specific DNA binding; DNA binding; transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; ubiquitin protein ligase binding; protein heterodimerization activity; E-box binding; p53 binding; protein domain specific binding; DNA-binding transcription factor activity, RNA polymerase II-specific; RNA polymerase II transcription regulatory region sequence-specific DNA binding;
Cellular component	cytoplasm; cytosol; nucleus; nuclear speck; motile cilium; transcription regulator complex; RNA polymerase II transcription regulator complex; axon cytoplasm; nucleoplasm; nuclear body; protein-containing complex;
Biological process	negative regulation of neuron apoptotic process; B-1 B cell homeostasis; regulation of transforming growth factor beta2 production; muscle cell cellular homeostasis; outflow tract morphogenesis; negative regulation of ossification; heart looping; negative regulation of TOR signaling; blood vessel development; hemoglobin biosynthetic process; angiogenesis; positive regulation of chemokine-mediated signaling pathway; positive regulation of insulin secretion involved in cellular response to glucose stimulus; positive regulation of hormone biosynthetic process; negative regulation of mesenchymal cell apoptotic process; regulation of aerobic respiration; positive regulation of neuroblast proliferation; dopaminergic neuron differentiation; lactate metabolic process; regulation of transcription, DNA-templated; blood vessel morphogenesis; positive regulation of erythrocyte differentiation; glucose homeostasis; vascular endothelial growth factor production; regulation of thymocyte apoptotic process; positive regulation of epithelial cell migration; negative regulation of thymocyte apoptotic process; transcription, DNA-templated; positive regulation of transcription, DNA-templated; axonal transport of mitochondrion; positive regulation of macroautophagy; cartilage development; positive regulation of nitric-oxide synthase activity; regulation of transcription from RNA polymerase II promoter in response to hypoxia; lactation; negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; positive regulation of pri-miRNA transcription by RNA polymerase II; digestive tract morphogenesis; cell differentiation; neural fold elevation formation; positive regulation of autophagy; retina vasculature development in camera-type eye; collagen metabolic process; embryonic placenta development; negative regulation of apoptotic process; positive regulation of angiogenesis; regulation of glycolytic process; epithelial to mesenchymal transition; cerebral cortex development; regulation of gene expression; positive regulation of chemokine production; intestinal epithelial cell maturation; regulation of catalytic activity; positive regulation of autophagy of mitochondrion; cardiac ventricle morphogenesis; response to muscle activity; epithelial cell differentiation involved in mammary gland alveolus development; visual learning; positive regulation of vascular endothelial growth factor receptor signaling pathway; negative regulation of bone mineralization; negative regulation of growth; response to hypoxia; positive regulation of endothelial cell proliferation; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; iris morphogenesis; mRNA transcription by RNA polymerase II; hypoxia-inducible factor-1alpha signaling pathway; vasculature development; regulation of cell population proliferation; neural crest cell migration; embryonic hemopoiesis; connective tissue replacement involved in inflammatory response wound healing; positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; negative regulation of reactive oxygen species metabolic process; positive regulation of vascular endothelial growth factor production; elastin metabolic process; positive regulation of glycolytic process; oxygen homeostasis; signal transduction; positive regulation of transcription by RNA polymerase II; cellular iron ion homeostasis; camera-type eye morphogenesis; cellular response to hypoxia; cellular response to interleukin-1; transcription by RNA polymerase II; protein deubiquitination; post-translational protein modification; response to iron ion; negative regulation of gene expression; positive regulation of blood vessel endothelial cell migration; positive regulation of gene expression; cytokine-mediated signaling pathway; regulation of transcription by RNA polymerase II; protein ubiquitination;
	Sources:Amigo / QuickGO
Orthologs
	3091
	15251
	ENSG00000100644
	ENSMUSG00000021109
	Q16665
	Q61221
	NM_181054; NM_001243084; NM_001530
	NM_010431; NM_001313919; NM_001313920
	NP_001230013; NP_001521; NP_851397; NP_001521.1
	NP_001300848; NP_001300849; NP_034561
	Wikidata
View/Edit Human	View/Edit Mouse

Hypoxia-inducible factor 1-alpha, also known as HIF-1-alpha, is a subunit of a heterodimeric transcription factor hypoxia-inducible factor 1 (HIF-1) that is encoded by the HIF1A gene.^[5]^[6]^[7] The Nobel Prize in Physiology or Medicine 2019 was awarded for the discovery of HIF.

HIF1A is a basic helix-loop-helix PAS domain containing protein, and is considered as the master transcriptional regulator of cellular and developmental response to hypoxia.^[8]^[9] The dysregulation and overexpression of HIF1A by either hypoxia or genetic alternations have been heavily implicated in cancer biology, as well as a number of other pathophysiologies, specifically in areas of vascularization and angiogenesis, energy metabolism, cell survival, and tumor invasion.^[7]^[10] The presence of HIF1A in a hypoxic environment is required to push forward normal placental development in early gestation. ^[11] Two other alternative transcripts encoding different isoforms have been identified.^[7]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000100644 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021109 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Semenza GL, Rue EA, Iyer NV, Pang MG, Kearns WG (June 1996). "Assignment of the hypoxia-inducible factor 1alpha gene to a region of conserved synteny on mouse chromosome 12 and human chromosome 14q". Genomics. 34 (3): 437–9. doi:10.1006/geno.1996.0311. PMID 8786149.
^ Hogenesch JB, Chan WK, Jackiw VH, Brown RC, Gu YZ, Pray-Grant M, Perdew GH, Bradfield CA (March 1997). "Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway". The Journal of Biological Chemistry. 272 (13): 8581–93. doi:10.1074/jbc.272.13.8581. PMID 9079689. S2CID 14908247.
^ ^a ^b ^c "Entrez Gene: HIF1A hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)".
^ Wang GL, Jiang BH, Rue EA, Semenza GL (June 1995). "Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension". Proceedings of the National Academy of Sciences of the United States of America. 92 (12): 5510–4. Bibcode:1995PNAS...92.5510W. doi:10.1073/pnas.92.12.5510. PMC 41725. PMID 7539918.
^ Iyer NV, Kotch LE, Agani F, Leung SW, Laughner E, Wenger RH, Gassmann M, Gearhart JD, Lawler AM, Yu AY, Semenza GL (January 1998). "Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1 alpha". Genes & Development. 12 (2): 149–62. doi:10.1101/gad.12.2.149. PMC 316445. PMID 9436976.
^ Semenza GL (October 2003). "Targeting HIF-1 for cancer therapy". Nature Reviews. Cancer. 3 (10): 721–32. doi:10.1038/nrc1187. PMID 13130303. S2CID 2448376.
^ Soares MJ (16 October 2017). "Hypoxia and Placental Development". Birth Defects Research. 109 (17): 4–6. doi:10.1002/bdr2.1135. PMC 5743230. PMID 29105383.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000100644 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000021109 – 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.

[pmid8786149-5] Semenza GL, Rue EA, Iyer NV, Pang MG, Kearns WG (June 1996). "Assignment of the hypoxia-inducible factor 1alpha gene to a region of conserved synteny on mouse chromosome 12 and human chromosome 14q". Genomics. 34 (3): 437–9. doi:10.1006/geno.1996.0311. PMID 8786149.

[pmid9079689-6] Hogenesch JB, Chan WK, Jackiw VH, Brown RC, Gu YZ, Pray-Grant M, Perdew GH, Bradfield CA (March 1997). "Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway". The Journal of Biological Chemistry. 272 (13): 8581–93. doi:10.1074/jbc.272.13.8581. PMID 9079689. S2CID 14908247.

[entrez-7] "Entrez Gene: HIF1A hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)".

[pmid7539918-8] Wang GL, Jiang BH, Rue EA, Semenza GL (June 1995). "Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension". Proceedings of the National Academy of Sciences of the United States of America. 92 (12): 5510–4. Bibcode:1995PNAS...92.5510W. doi:10.1073/pnas.92.12.5510. PMC 41725. PMID 7539918.

[9] Iyer NV, Kotch LE, Agani F, Leung SW, Laughner E, Wenger RH, Gassmann M, Gearhart JD, Lawler AM, Yu AY, Semenza GL (January 1998). "Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1 alpha". Genes & Development. 12 (2): 149–62. doi:10.1101/gad.12.2.149. PMC 316445. PMID 9436976.

[Semenza_2003-10] Semenza GL (October 2003). "Targeting HIF-1 for cancer therapy". Nature Reviews. Cancer. 3 (10): 721–32. doi:10.1038/nrc1187. PMID 13130303. S2CID 2448376.

[11] Soares MJ (16 October 2017). "Hypoxia and Placental Development". Birth Defects Research. 109 (17): 4–6. doi:10.1002/bdr2.1135. PMC 5743230. PMID 29105383.

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