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SOCS3 — TCEB1
Pathways - manually collected, often from reviews:
-
Reactome Reaction:
SOCS3
→
TCEB1
(indirect_complex)
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
SOCS3
—
TCEB1
(physical association, affinity chromatography technology)
Zhang et al., J Biol Chem 2012*
-
IRef Biogrid Interaction:
SOCS3
—
TCEB1
(physical association, affinity chromatography technology)
Xiao et al., FASEB J 2007*
-
IRef Biogrid Interaction:
SOCS3
—
TCEB1
(direct interaction, pull down)
Haan et al., J Biol Chem 2003*
-
IRef Biogrid Interaction:
SOCS3
—
TCEB1
(physical association, affinity chromatography technology)
Haan et al., J Biol Chem 2003*
-
IRef Biogrid Interaction:
SOCS3
—
TCEB1
(physical association, affinity chromatography technology)
Kamura et al., Genes Dev 2004
-
IRef Hprd Interaction:
SOCS3
—
TCEB1
(in vitro)
Zhang et al., Proc Natl Acad Sci U S A 1999*
-
IRef Hprd Interaction:
SOCS3
—
TCEB1
(in vivo)
Zhang et al., Proc Natl Acad Sci U S A 1999*
-
IRef Intact Interaction:
Complex of 11 proteins
(association, anti tag coimmunoprecipitation)
Kamura et al., Genes Dev 2004
-
IRef Ophid Interaction:
SOCS3
—
TCEB1
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Haan et al., J Biol Chem 2003
:
In the present study, we have found that phosphorylation of
SOCS3 at two tyrosine residues in the conserved SOCS box, Tyr204 and Tyr221, can
inhibit the
SOCS3-elongin C interaction and activate proteasome mediated SOCS3 degradation ... The data suggest that interaction with
elongin C stabilizes
SOCS3 protein expression and that phosphorylation of SOCS box tyrosine residues disrupts the complex and enhances proteasome mediated degradation of SOCS3
Tannahill et al., Mol Cell Biol 2005
:
Furthermore, we provide evidence that this degradation is dependent on the presence of an intact SOCS box and that the loss of
SOCS3 is
enhanced by coexpression of
elongin B/C