Table 7.

Post-translational modification (PTM) of HIF-1α.

Interactor	Site of PTM (AA#)*	Type of PTM	Consequence	Ref
ATM	696	Phosphorylation	Stabilization	[158]
CBX4	391,477	Sumoylation	Transactivation	[18]
CDK1	668	Phosphorylation	Stabilization	[22]
CDK5	687	Phosphorylation	Stabilization	[25]
CK1δ	247	Phosphorylation	Dimerization blocked	[29,159]
CK2	796	Phosphorylation	Transactivation	[160,161]
ERK1/2	641,643	Phosphorylation	Nuclear localization	[32]
GSK-3β	551.555,589	Phosphorylation	Degradation	[49]
HDAC4	10,11,12,19,21	Deacetylation	Stabilization	[55]
LSD1	32	Demethylation	Stabilization	[161]
P300	709	Acetylation	Stabilization	[55]
PCAF	674	Acetylation	Transactivation	[99]
PIASY	ND (not 391,477)	Sumoylation	Degradation	[104]
PLK3	576,657	Phosphorylation	Degradation	[108]
PRKACA	63,692	Phosphorylation	Degradation	[111]
SENP1	ND	Desumoylation	Stabilization	[126]
SET7	32	Methylation	Repression	[129]
SET7	32	Methylation	Degradation	[161]
SIRT1	674	Deacetylation	Repression	[99]
SIRT2	709	Deacetylation	Degradation	[131]
STUB1	ND	Ubiquitination	Degradation	[64]
TRAF6	ND	Ubiquitinationa	Stabilization	[144]
VHL	532,538,547	Ubiquitination*	Degradation	[162]

^*(AA#), the amino acid number of the HIF-1α residue that is subject to PTM is shown, based on GenBank accession number U22431.1.

^*K48-linked polyubiquitination.

^aK63-linked polyubiquitination.