Literature summary for 1.14.11.30 extracted from

Lando, D.; Peet, D.J.; Whelan, D.A.; Gorman, J.J.; Whitelaw, M.L.
Asparagine hydroxylation of the HIF transactivation domain: A hypoxic switch (2002), Science, 295, 858-861.

Search for more literature for 1.14.11.30

Application

Application	Comment	Organism
medicine	the high constitutive activities of the proteins with both Pro and Asn substitutions confirm that the relevant prolyl and asparaginyl hydroxylases are attractive targets for therapeutic regulation of hypoxia-inducible factor-1alpha and hypoxia-inducible factor-2alpha	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2	Homo sapiens	-	hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2	-	Homo sapiens	hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2	-	?

General Information

General Information	Comment	Organism
physiological function	there are at least two major steps involved in the hypoxic induction of the HIF proteins: (i) inhibition of oxygen-dependent hydroxylation on Pro residues in the oxygen-dependent degradation domain to prevent interaction of HIF with the von Hippel-Lindau tumor suppressor/ubiquitin ligase complex and thus avoid proteasomal destruction, and (ii) inhibition of oxygen-dependent hydroxylation of Asn in the COOH-terminal transactivation domain to promote interaction with the p300/CBP coactivator and induce transcription	Homo sapiens

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Release 2023.1 (January 2023)