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NDUFA13 — STAT3
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind_translation Interaction:
NDUFA13
—
STAT3
(coimmunoprecipitation)
Lufei et al., EMBO J 2003*
-
IRef Biogrid Interaction:
NDUFA13
—
STAT3
(physical association, affinity chromatography technology)
Zhang et al., Proc Natl Acad Sci U S A 2003*
-
IRef Biogrid Interaction:
NDUFA13
—
STAT3
(direct interaction, two hybrid)
Zhang et al., Proc Natl Acad Sci U S A 2003*
-
IRef Hprd Interaction:
STAT3
—
NDUFA13
(in vivo)
Lufei et al., EMBO J 2003*, Zhang et al., Proc Natl Acad Sci U S A 2003*
-
IRef Hprd Interaction:
STAT3
—
NDUFA13
(in vitro)
Lufei et al., EMBO J 2003*, Zhang et al., Proc Natl Acad Sci U S A 2003*
-
IRef Hprd Interaction:
STAT3
—
NDUFA13
(two hybrid)
Lufei et al., EMBO J 2003*, Zhang et al., Proc Natl Acad Sci U S A 2003*
-
IRef Intact Interaction:
Complex of 306 proteins
(association, pull down)
Komarova et al., Mol Cell Proteomics 2011
Text-mined interactions from Literome
Lufei et al., EMBO J 2003
:
GRIM-19 , a death-regulatory gene product,
suppresses Stat3 activity via functional interaction ...
GRIM-19 represses
Stat3 transcriptional activity and its target gene expression, and also suppresses cell growth in Src transformed cells and a Stat3 expressing cell line
Shulga et al., J Cell Sci 2012
(Necrosis) :
GRIM-19 mediated translocation of
STAT3 to mitochondria is necessary for TNF induced necroptosis ... The phosphorylation of
STAT3 induces interaction with
GRIM-19 , a subunit of mitochondrial complex I, with a resultant translocation of STAT3 to the mitochondria, where it induces an increase in reactive oxygen species production and cell death
Bu et al., Gene 2013
(Stomach Neoplasms) :
Finally, we demonstrate that expression of
GRIM-19 in BGC-803 cells
suppresses accumulation of
STAT3