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DDB1 — STAT1
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
STAT1
—
DDB1
(physical association, affinity chromatography technology)
Wang et al., Molecular systems biology 2011
-
IRef Biogrid Interaction:
STAT1
—
DDB1
(direct interaction, two hybrid)
Wang et al., Molecular systems biology 2011
-
IRef Intact Interaction:
STAT1
—
DDB1
(physical association, pull down)
Wang et al., Molecular systems biology 2011
-
IRef Intact Interaction:
STAT1
—
DDB1
(physical association, two hybrid)
Wang et al., Molecular systems biology 2011
-
IRef Intact Interaction:
Complex of 244 proteins
(association, pull down)
Komarova et al., Mol Cell Proteomics 2011
Text-mined interactions from Literome
Andrejeva et al., J Virol 2002
(Xeroderma Pigmentosum) :
Furthermore, STAT1 is degraded in GM02415 ( 2RO ) cells, which have a mutation in DDB2 ( the p48 subunit of DDB ) which abolishes its ability to interact with DDB1, thereby demonstrating that the
role of
DDB1 in
STAT1 degradation is independent of its association with DDB2
Ulane et al., Virology 2002
:
The
roles of both
DDB1 and Cul4A in
STAT1 degradation by SV5 infection were analyzed using small interfering RNAs