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Review
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p(HGNC:VHL) => deg(p(HGNC:HIF1A))
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Approximately 2000 hand curated statements drawn from 57 PubMeds.
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Copyright (c) 2011-2012, Selventa. All Rights Reserved.
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BEL Framework Small Corpus Document
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Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License
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Hydroxylation at two prolyl residues (Pro402 and Pro564 in human HIF-1α) mediates
interactions with the von Hippel-Lindau (VHL) E3 ubiquitin ligase complex that
targets HIF-α for proteasomal destruction28, 29, 30, 34. Each site can interact
independently with VHL E3, potentially contributing to the extremely rapid proteolysis
of HIF-α that is observed in oxygenated cells34. These sites contain a conserved
LxxLAP motif and are targeted by a newly defined prolyl hydroxylase activity,
that in mammalian cells is provided by three isoforms termed PHD (prolyl hydroxylase
domain) 1-3 (refs. 31,32).
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2014-07-03T14:29:32.242+02:00
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