Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains.

Journal article

Factor-inhibiting hypoxia-inducible factor (FIH) is an Fe(II)/2-oxoglutarate-dependent dioxygenase that acts as a negative regulator of the hypoxia-inducible factor (HIF) by catalysing β-hydroxylation of an asparaginyl residue in its C-terminal transcriptional activation domain (CAD). In addition to the hypoxia-inducible factor C-terminal transcriptional activation domain (HIF-CAD), FIH also catalyses asparaginyl hydroxylation of many ankyrin repeat domain-containing proteins, revealing a bro...

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Authors: Yang, M; Chowdhury, R; Ge, W; Hamed, R; McDonough, M

• Publication status: Published
• Journal: FEBS journal
• Volume: 278
• Issue: 7
• Pages: 1086-1097
• Publication date: 2011-04-01
• DOI: 10.1111/j.1742-4658.2011.08022.x
• EISSN: 1742-4658
• ISSN: 1742-464X
• Language: English
• Keywords: Amino Acid Sequence; Molecular Sequence Data; Models, Molecular; Ankyrin Repeat; HEK293 Cells; Humans; Mixed Function Oxygenases; Tankyrases; Sequence Alignment; Protein Structure, Tertiary; Mass Spectrometry; Histidine; Repressor Proteins; Hydroxylation; Protein Processing, Post-Translational