Positive Samples: Mouse skeletal muscle
HIF prolyl hydroxylase 3 is a prolyl hydroxylase that modifies HIF-alpha. Classic prolyl hydroxylases are found in the endoplasmic reticulum and modify collagen, whereas HIF is an intracellular protein and the HPH sites do not resemble those modifying collagen. HIF is a transcriptional complex that plays a critical role in oxygen homeostasis. HPH is an essential component of the pathway through which cells sense oxygen. In the presence of oxygen, HPHs convert specific prolyl residues in HIF-alpha to hydroxyproline, leading to HIF-alpha destruction. Low oxygen levels, sensed at the cellular level, cause the HIF conversion to be reduced so that HIF is stable and there is increased angiogenesis. HIF prolyl hydroxylase 1, specifically, catalyzes the posttranslational formation of 4-hydroxyproline in HIF alpha proteins. It hydroxylates HIF-1 alpha at Pro(564) and HIF-2 alpha. It targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitylation complex. It may also play a role in cell growth regulation in muscle cells and in apoptosis in neuronal tissues, promoting cell death through a caspase-dependent mechanism.
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Protein Aliases: Parvalbumin (calcium binding protein); Parvalbumin alpha
Gene Aliases: D22S749; PALB1; Parv; PV; Pva; PVALB