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. Author manuscript; available in PMC: 2015 Feb 27.
Published in final edited form as: Crit Rev Biochem Mol Biol. 2013 Oct 7;49(1):1–15. doi: 10.3109/10409238.2013.838205

Figure 1.

Figure 1

HIF protein domains and post-translational modifications. The HIF proteins are comprised of several conserved domains that are involved in DNA binding (basic Helix-Loop-Helix, bHLH), protein-protein interactions and dimerization (PER-ARNT-SIM, PAS-A, PAS-B, and PAS-associated C-terminal domain), oxygen-dependent degradation (ODD) and transcriptional activation (N-TAD, C-TAD). Numerous HIF3A isoforms exist, with several longer forms possessing transactivation and leucine zipper (LZIP) domains (HIF3A-1) while others lack any known transactivation domains and act as negative regulators (HIF3A-4). Multiple post-translational modifications are known to modulate HIF protein stability and transcriptional activity. Selected modifications are shown here along with the enzyme responsible and the overall positive (+) or negative (−) effects on HIF transcriptional function.