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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