1.14.11.29	hypoxia-inducible factor 1 alpha-L-proline + 2-oxoglutarate + O2	-	
1.14.11.29	hypoxia-inducible factor 1alpha-L-proline + 2-oxoglutarate + O2	-	
1.14.11.29	hypoxia-inducible factor-alpha-L-proline + 2-oxoglutarate + O2	-	
1.14.11.29	hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2	-	
1.14.11.29	hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2	HIF (hypoxia-inducible factor) is a transcription factor that plays a pivotal role in cellular adaptation to changes in oxygen availability. In the presence of oxygen, HIF is targeted for destruction by an E3 ubiquitin ligase containing the von Hippel-Lindau tumor suppressor protein (pVHL). Human pVHL binds to a short HIF-derived peptide when a conserved proline residue at the core of this peptide is hydroxylated. This protein modifiation may play a key role in mammalian oxygen sensing	
1.14.11.29	hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2	hypoxia-inducible factor (HIF) is a transcriptional complex that plays a central role in the regulation of gene expression by oxygen. In oxygenated and iron replete cells, HIF-alpha subunits are rapidly destroyed by a mechanism that involves ubiquitylation by the von Hippel-Lindau tumor suppressor (pVHL) E3 ligase complex. This process is suppressed by hypoxia and iron chelation, allowing transcriptional activation. The interaction between human pVHL and a specific domain of the HIF-1alpha subunit is regulated through hydroxylation of a proline residue (HIF-1alpha P564) by HIF-alpha prolyl-hydroxylase (HIF-PH). HIF-PH functions directly as a cellular oxygen sensor	
1.14.11.29	hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2	mammalian cells respond to changes in oxygen availability through a conserved pathway that is regulated by the hypoxia-inducible factor (HIF). The alpha subunit of the hypoxia-inducible factor is targeted for degradation under normoxic conditions by a ubiquitin-ligase complex that recognizes a hydroxylated proline residue in hypoxia-inducible factor. HIF prolyl hydroxylase is responsible for this posttranslational modification	
1.14.11.29	hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2	mammalian cells respond to changes in oxygen availability through a conserved pathway that is regulated by the hypoxia-inducible factor (HIF). The alpha subunit of the hypoxia-inducible factor is targeted for degradation under normoxic conditions by a ubiquitin-ligase complex that recognizes a hydroxylated proline residue in hypoxia-inducible factor. HIF prolyl is responsible for this posttranslational modification	
1.14.11.29	hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2	HIF1alpha is a better substrate than HIF2alpha for PHD2	
1.14.11.29	hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2	PHD enzymes hydroxylates HIF-alpha at prolyl residues present in the transcriptional activation domain N-TAD