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CCNB2 — CDK1

Pathways - manually collected, often from reviews:

• KEGG Cell cycle: Complex of CCNB1-CCNB2-CCNB3-CDK1 → PLK1 (protein-protein, phosphorylation)
• KEGG Cell cycle: Complex of 14 proteins → Complex of CCNB1-CCNB2-CCNB3-CDK1 (protein-protein, inhibition)
  
• KEGG Oocyte meiosis: Complex of CCNB2-CDK1 → SLK (protein-protein, activation)
• KEGG Oocyte meiosis: Complex of CCNB2-CDK1 → CDC25C (protein-protein, activation)
• KEGG Oocyte meiosis: Complex of CCNB2-CDK1 → CPEB1 (protein-protein, activation)
• KEGG p53 signaling pathway: SFN → Complex of CCNB1-CCNB2-CCNB3-CDK1 (protein-protein, inhibition)
  
• KEGG p53 signaling pathway: GADD45A/GADD45B/GADD45G → Complex of CCNB1-CCNB2-CCNB3-CDK1 (protein-protein, inhibition)
  
• Reactome Reaction: CDK1 → CCNB2 (direct_complex) Pines et al., J Cell Biol 1991*
• Reactome Reaction: CDK1 → CCNB2 (reaction) Pines et al., J Cell Biol 1991*
• WikiPathways miRNA Regulation of DNA Damage Response: Complex of CCNB1-CCNB3-CCNB2 → CDK1 (activation)
• WikiPathways DNA Damage Response: Complex of CCNB1-CCNB3-CCNB2 → CDK1 (activation)

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Bind Interaction: CCNB2 — CDK1 Jackman et al., EMBO J 1995
• IRef Bind Interaction: CCNB2 — CDK1 Pines et al., EMBO J 1994*
• IRef Bind_translation Interaction: CCNB2 — CDK1 (coimmunoprecipitation) Pines et al., EMBO J 1994*
• IRef Bind_translation Interaction: CCNB2 — CDK1 (coimmunoprecipitation) Jackman et al., EMBO J 1995
• MIPS CORUM Cell cycle kinase complex CDC2: Cell cycle kinase complex CDC2 complex (CCNB1-CCNB2-CCND1-CDK1-CDKN1A-PCNA) Zhang et al., Mol Biol Cell 1993
• MIPS CORUM CCNB2-CDC2 complex: CCNB2-CDC2 complex complex (CCNB2-CDK1) Pines et al., EMBO J 1994*
• IRef Corum Interaction: CCNB2 — CDK1 (association, coimmunoprecipitation) Pines et al., EMBO J 1994*
• IRef Corum Interaction: Complex of CCNB2-CDKN1A-CCNB1-PCNA-CDK1-CCND1 (association, anti bait coimmunoprecipitation) Zhang et al., Mol Biol Cell 1993
• IRef Hprd Interaction: Complex of TGFBR2-CCNB2-TGFBR2-CDK1-CDK1-CCNB2-CDK1-CCNB2-TGFBR2 (in vivo) Liu et al., Oncogene 1999*
• IRef Hprd Interaction: CCNB2 — CDK1 (in vivo) Liu et al., Oncogene 1999*
• IRef Hprd Interaction: CCNB2 — CDK1 (in vitro) Liu et al., Oncogene 1999*
• IRef Intact Interaction: Complex of CCNB1-CDK1-CCNB2 (phosphorylation reaction, protein kinase assay) Cheng et al., Cell 2009*
• IRef Intact Interaction: Complex of PKMYT1-CKS2-CCNB2-CKS1B-CCNA2-CDK1-CCNB1-CDKN1B-CDKN1A (association, tandem affinity purification) Varjosalo et al., Cell reports 2013
• IRef Intact Interaction: CCNB2 — CDK1 (direct interaction, inferred by curator) Hermjakob et al., Nucleic Acids Res 2004
• IRef Ophid Interaction: CCNB2 — CDK1 (aggregation, confirmational text mining) Liu et al., Oncogene 1999*
• IRef Ophid Interaction: CCNB2 — CDK1 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Borgne et al., J Biol Chem 1999 : We demonstrate that Cdc2 itself is the cyclin B kinase ; cyclin B phosphorylation requires Cdc2 activity both in vivo ( sensitivity to vitamin K3, a Cdc25 inhibitor ) and in vitro ( copurification with Cdc2-cyclin B, requirement of Cdc2 dephosphorylation, and sensitivity to chemical inhibitors of cyclin dependent kinases )
Qian et al., Mol Cell Biol 1999 : In addition, during anaphase T201D Plx1 reduced preferentially the degradation of cyclin B2 and delayed the reduction in Cdc2 histone H1 kinase activity
Li et al., Cell Signal 2006 : Activation of cdk1 : : cyclinB1 was coincident with I-2 phosphorylation, but neither MAPK nor GSK3 were phosphorylated at this time, so we concluded that in living cells only cdk1 : : cyclinB1 phosphorylated the PXTP site in I-2