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Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.

Abstract:

Post-translational hydroxylation has been considered an unusual modification on intracellular proteins. However, following the recognition that oxygen-sensitive prolyl and asparaginyl hydroxylation are central to the regulation of the transcription factor hypoxia-inducible factor (HIF), interest has centered on the possibility that these enzymes may have other substrates in the proteome. In support of this certain ankyrin repeat domain (ARD)-containing proteins, including members of the Ikapp...

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Publication status:
Published

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Publisher copy:
10.1074/mcp.m800340-mcp200

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, CCMP
Kramer, HB More by this author
Kessler, BM More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, CCMP, Biomedical Research Centre
Journal:
Molecular and cellular proteomics : MCP
Volume:
8
Issue:
3
Pages:
535-546
Publication date:
2009-03-05
DOI:
EISSN:
1535-9484
ISSN:
1535-9476
URN:
uuid:943e56b5-cdf0-4299-ab9c-2c2d3730c5b6
Source identifiers:
2553
Local pid:
pubs:2553

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