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Proteins/UNIPROT:Q9NWT6
Hydroxylates HIF-1 alpha at 'Asn-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation..
Function from UniProtKB (Q9NWT6), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
332 statements
332 statements · 5 reference databases · Subject: HIF1AN · Sources: gene ontology, Hetionet, Reactome, UniProt, WikiPathways · Rows fetched: 300
5 reactions
2-oxoglutarate(2-)+dioxygen+MAM02702ccarbon dioxide+MAM02701c+succinate(2-)
Reaction pageLeft to rightBalance undeterminableEC 1.14.11.16cytosol
Human-GEM MAR09532CC BY 4.0Reference data
L-histidyl-[ankyrin-repeat domain protein]+2-oxoglutarate(2-)+dioxygen(3S)-3-hydroxy-L-histidyl-[ankyrin-repeat domain protein]+
4 names
Resolves to: HIF1AN
Catalysed by HIF1AN
Reaction pageDirection not assertedBalance undeterminable
Rhea RHEA:54264CC BY 4.0Reference data
L-asparaginyl-[hypoxia-inducible factor alpha subunit]+2-oxoglutarate(2-)+dioxygen(3S)-3-hydroxy-L-asparaginyl-[hypoxia-inducible factor alpha subunit]+succinate(2-)+carbon dioxide
Catalysed by HIF1AN
Reaction pageDirection not assertedBalance undeterminable
Rhea RHEA:54268CC BY 4.0Reference data
L-asparaginyl-[ankyrin-repeat domain protein]+2-oxoglutarate(2-)+dioxygen(3S)-3-hydroxy-L-asparaginyl-[ankyrin-repeat domain protein]+succinate(2-)+carbon dioxide
Catalysed by HIF1AN
Reaction pageDirection not assertedBalance undeterminable
Rhea RHEA:54272CC BY 4.0Reference data
L-aspartyl-[ankyrin-repeat domain protein]+2-oxoglutarate(2-)+dioxygen(3S)-3-hydroxy-L-aspartyl-[ankyrin-repeat domain protein]+succinate(2-)+carbon dioxide
Catalysed by HIF1AN
Reaction pageDirection not assertedBalance undeterminable
Rhea RHEA:54280CC BY 4.0Reference data