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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