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Switch #:
SWTI000023
Switch type:
Binary
Switch subtype:
Physicochemical compatibility

Description:
Hydroxylation of P564 in the VHL-binding motif of Hypoxia-inducible factor 1-alpha (HIF1A) induces binding to the Von Hippel-Lindau disease tumor suppressor (VHL) protein.

Participants:
(1) Hypoxia-inducible factor 1-alpha (HIF1A)
(2) Von Hippel-Lindau disease tumor suppressor (VHL)

Interactions
Interaction #1 HIF1A - VHL

Interfaces
(1) DEG_ODPH_VHL_1 motif (562LAPYIPMDDDFQL574) in Hypoxia-inducible factor 1-alpha (HIF1A)
(2) von Hippel-Lindau disease tumour suppressor protein (58-213) in Von Hippel-Lindau disease tumor suppressor (VHL)

Interaction Regulation
PTM-dependent Induction (MOD:00678 at P564 on Hypoxia-inducible factor 1-alpha (HIF1A)) of the Hypoxia-inducible factor 1-alpha (HIF1A) DEG_ODPH_VHL_1 motif - Von Hippel-Lindau disease tumor suppressor (VHL) von Hippel-Lindau disease tumour suppressor protein interaction

Regulatory Enzymes for switch
Modifying enzymes for residue: P564: Egl nine homolog 1 (EGLN1)

Additional Information
Structural information: 1LM8, 1LQB
Context
References

(1) Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL.
Hon et al. Nature (2002)

(2) Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor.
Hirsilä et al. J. Biol. Chem. (2003)

See also

Other switches involving participants
Hypoxia-inducible factor 1-alpha (HIF1A) - 2 more (view)
Von Hippel-Lindau disease tumor suppressor (VHL) - 5 more (view)

Other switches involving interfaces
DEG_ODPH_VHL_1 - 5 more (view)
von Hippel-Lindau disease tumour suppressor protein - 5 more (view)




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