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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:P40337 (6 hits) x


x  Coloured by switch type.
  Domain hiding  Altered binding specificity  Motif hiding  Composite binding site formation
  Uncategorised  Rheostatic  Allostery  Avidity-sensing
  Physicochemical compatibility  Pre-translational  Competition

x  Index
Endothelial PAS domain-containing protein 1Hypoxia-inducible factor 1-alphaHypoxia-inducible factor 3-alpha


MotifStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

Endothelial PAS domain-containing protein 1 - EPAS1 -  Homo sapiens
DEG_ODPH_VHL_1403416BinaryPhysicochemical compatibilityHydroxylation of P405 in the VHL-binding motif of Endothelial PAS domain-containing protein 1 (EPAS1) induces binding to the Von Hippel-Lindau disease tumor suppressor (VHL) protein.
details
DEG_ODPH_VHL_1529542BinaryPhysicochemical compatibilityHydroxylation of P531 in the VHL-binding motif of Endothelial PAS domain-containing protein 1 (EPAS1) induces binding to the Von Hippel-Lindau disease tumor suppressor (VHL) protein.
details

Hypoxia-inducible factor 1-alpha - HIF1A -  Homo sapiens
DEG_ODPH_VHL_1400413BinaryPhysicochemical compatibilityHydroxylation of P402 in the VHL-binding motif of Hypoxia-inducible factor 1-alpha (HIF1A) induces binding to the Von Hippel-Lindau disease tumor suppressor (VHL) protein.
details
DEG_ODPH_VHL_1562574BinaryPhysicochemical compatibilityHydroxylation 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.
details

Hypoxia-inducible factor 3-alpha - HIF3A -  Homo sapiens
DEG_ODPH_VHL_1490502BinaryPhysicochemical compatibilityHydroxylation of P492 in the VHL-binding motif of Hypoxia-inducible factor 3-alpha (HIF3A) induces binding to the Von Hippel-Lindau disease tumor suppressor (VHL) protein.
details
DEG_ODPH_VHL_1490502BinaryPre‑translationalAlternative splicing removes the VHL-hydroxyproline-modified binding motif of Hypoxia-inducible factor 3-alpha (HIF3A), abrogating binding to Von Hippel-Lindau disease tumor suppressor (VHL). Other studies have shown that the HIF-3 alpha-4 splice variant (Isoform HIF-3alpha4 of Hypoxia-inducible factor 3-alpha (HIF3A)) can act as a dominant negative form with tumour-suppressive activity (see Maynard et al. (2007) (here)).
details
           
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