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HIPK2 — PML

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: HIPK2 — PML (physical association, affinity chromatography technology) de la Vega et al., Biochim Biophys Acta 2011*
• IRef Biogrid Interaction: HIPK2 — PML (direct interaction, enzymatic study) Renner et al., Mol Cell 2010*
• IRef Biogrid Interaction: HIPK2 — PML (physical association, affinity chromatography technology) Sung et al., Exp Cell Res 2011*
• IRef Biogrid Interaction: HIPK2 — PML (colocalization, imaging technique) Sung et al., Exp Cell Res 2011*
• IRef Biogrid Interaction: HIPK2 — PML (physical association, affinity chromatography technology) Gresko et al., Oncogene 2009*
• IRef Biogrid Interaction: HIPK2 — PML (direct interaction, enzymatic study) Gresko et al., Oncogene 2009*

Text-mined interactions from Literome

Weidtkamp-Peters et al., J Cell Sci 2008 : HIPK2 requires an active kinase for PML NB targeting and elevated levels of PML IV increase its residence time
Shima et al., Mol Cell Biol 2008 (Leukemia) : In contrast, the leukemia associated fusion PML-RARalpha induced the degradation of HIPK2
Gresko et al., Oncogene 2009 : Although HIPK2 mediated phosphorylation of PML occurs early during the DNA damage response, the oncogenic PML-RARalpha fusion protein is phosphorylated with significantly delayed kinetics