◀ Back to CDK2
CDK2 — MYBL2
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
MYBL2
—
CDK2
(direct interaction, enzymatic study)
Bartsch et al., Eur J Biochem 1999*
-
IRef Biogrid Interaction:
MYBL2
—
CDK2
(direct interaction, enzymatic study)
Johnson et al., J Biol Chem 1999*
-
IRef Biogrid Interaction:
MYBL2
—
CDK2
(direct interaction, enzymatic study)
Müller-Tidow et al., Blood 2001*
-
IRef Hprd Interaction:
MYBL2
—
CDK2
(in vivo)
Bartsch et al., Eur J Biochem 1999*, Johnson et al., J Biol Chem 1999*, Saville et al., Oncogene 1998*
-
IRef Hprd Interaction:
MYBL2
—
CDK2
(in vitro)
Bartsch et al., Eur J Biochem 1999*, Johnson et al., J Biol Chem 1999*, Saville et al., Oncogene 1998*
Text-mined interactions from Literome
Bessa et al., Oncogene 2001
(Bone Neoplasms...) :
The importance of this modification was first emphasized by showing that co-transfected dominant negative
Cdk2 ( Cdk2DN ) substantially
reduced B-Myb transactivation activity ... We also found that
B-Myb could synergize with the CBP coactivator and that this cooperativity was cyclin
A/Cdk2 dependent
Ziebold et al., Curr Biol 1997
:
Phosphorylation and
activation of
B-Myb by cyclin
A-Cdk2
Lane et al., Oncogene 1997
:
Previously, we have shown that
B-Myb is specifically phosphorylated during S-phase and that similar modification to a less electrophoretically mobile form could be
induced by baculovirus expressed cyclin
A/Cdk2 kinase ... Whereas wild-type
B-Myb transactivation activity could not be
potentiated by cyclin
A/Cdk2 in NIH3T3 cells, the truncated protein was hyperactive
Saville et al., Oncogene 1998
(Bone Neoplasms...) :
Consistent with this notion, the S phase-specific cyclin
A/Cdk2 was found previously to
enhance B-Myb transactivation activity in cotransfected cells ... In this study we provide evidence that
B-Myb is a direct physiological
target for cyclin
A/Cdk2