◀ Back to CCNE2

CCNE2 — CDK2

Pathways - manually collected, often from reviews:

• OpenBEL Selventa BEL large corpus: CDK2 → Complex of CCNE2-CDK2 (directlyIncreases, CCNE2/CDK2 Activity)
  Evidence: Fig. (4). Physical and functional interactions between components of the cell cycle and transcription factors. The cyclin D1/CDK4 complex is shown in relation to its substrate pRB. In addition, cyclin D1 binds to the HAT domain of P/CAF [10] and to the p160 coactivator SRC1 [15]. Cyclin D1 and cyclin E both regulate the cell cycle arrest function of BRG1 [178]. Cyclin D1 overcomes the BRCA1-mediated inhibition of liganded ER?. Cyclin E/CDK2 phosphorylates NPAT, which in turn contributes to the i...
• OpenBEL Selventa BEL large corpus: CDK2 → Complex of CCNE2-CDK2 (directlyIncreases, CCNE2/CDK2 Activity)
  Evidence: E2 sensitivity is regulated by acetylation of lysines 302 and 303, by CREB-binding protein (CBP).
• OpenBEL Selventa BEL large corpus: RB1 → Complex of CCNE2-CDK2 (increases, RB1 Activity)
  Evidence: The primary substrates of CDK4/6 and CDK2 in G1 progression are the members of the retinoblastoma protein family RB,p107 and p130 The activity of the RB proteins is modulated by sequential phosphorylation by CDK4/6cyclinD and CDK2cyclinE complexes
• KEGG Cell cycle: Complex of CCNE1-CCNE2-CDK2 → CDKN1B/CDKN1C (protein-protein, inhibition)
• KEGG Cell cycle: CDKN1A → Complex of CCNE1-CCNE2-CDK2 (protein-protein, inhibition)
  
• KEGG Cell cycle: Complex of CUL1-RBX1-SKP1-SKP2 → Complex of CCNE1-CCNE2-CDK2 (protein-protein, inhibition)
  
• KEGG Cell cycle: Complex of CCNE1-CCNE2-CDK2 → RB1 (protein-protein, inhibition)
• KEGG Oocyte meiosis: Complex of CCNE1-CCNE2-CDK2 → ANAPC1/ANAPC10/ANAPC11/ANAPC13/ANAPC2/ANAPC4/ANAPC5/ANAPC7/CDC16/CDC23/CDC26/CDC27 (protein-protein, inhibition)
  
• KEGG p53 signaling pathway: CDKN1A → Complex of CCNE1-CCNE2-CDK2 (protein-protein, inhibition)
  
• KEGG Pathways in cancer: Complex of CCNE1-CCNE2-CDK2 → RB1 (protein-protein, activation)
• KEGG Pathways in cancer: CDKN1B → Complex of CCNE1-CCNE2-CDK2 (protein-protein, inhibition)
  
• KEGG Prostate cancer: Complex of CCNE1-CCNE2-CDK2 → RB1 (protein-protein, activation)
• KEGG Prostate cancer: CDKN1B → Complex of CCNE1-CCNE2-CDK2 (protein-protein, missing interaction)
  
• KEGG Small cell lung cancer: Complex of CCNE1-CCNE2-CDK2 → RB1 (protein-protein, activation)
• KEGG Small cell lung cancer: CDKN1B → Complex of CCNE1-CCNE2-CDK2 (protein-protein, inhibition)
  
• NCI Pathway Database p73 transcription factor network: Cyclin B/CDK1-2 complex (CCNE2-CDK1_CDK2) → TAp73b (tetramer) complex (TP73) (modification, activates)
  Gaiddon et al., J Biol Chem 2003, Fulco et al., J Biol Chem 2003*
  Evidence: mutant phenotype, assay, physical interaction
• NCI Pathway Database p73 transcription factor network: Cyclin E/CDK2 complex (CCNE2-CDK2) → TAp73b (tetramer) complex (TP73) (modification, activates)
  Gaiddon et al., J Biol Chem 2003
  Evidence: mutant phenotype, assay, physical interaction
• Reactome Reaction: CDK2 → CCNE2 (direct_complex) Aprelikova et al., J Biol Chem 1995, Desai et al., Mol Cell Biol 1995
• Reactome Reaction: CDK2 → CCNE2 (reaction) Desai et al., Mol Cell Biol 1995
• WikiPathways miRNA Regulation of DNA Damage Response: Complex of CDK4-CCND1-CDK6-CCND2-CCND3-CDK5 → Complex of CDK2-CCNE2-CCNE1 (inhibition)
  
• WikiPathways miRNA Regulation of DNA Damage Response: CDKN1A → Complex of CDK2-CCNE2-CCNE1 (inhibition)
  
• WikiPathways DNA Damage Response: Complex of CDK4-CCND1-CDK6-CCND2-CCND3-CDK5 → Complex of CDK2-CCNE2-CCNE1 (inhibition)
  
• WikiPathways DNA Damage Response: CDKN1A → Complex of CDK2-CCNE2-CCNE1 (inhibition)
  

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

Studies that report less than 10 interactions are marked with *

• IRef Bind Interaction: CDK2 — CCNE2 Ramachandran et al., Science 2004
• IRef Bind_translation Interaction: CDK2 — CCNE2 (array technology) Ramachandran et al., Science 2004
• IRef Biogrid Interaction: CCNE2 — CDK2 (physical association, affinity chromatography technology) Gudas et al., Mol Cell Biol 1999*
• IRef Biogrid Interaction: CCNE2 — CDK2 (physical association, affinity chromatography technology) Varjosalo et al., Nat Methods 2013
• IRef Biogrid Interaction: CCNE2 — CDK2 (physical association, affinity chromatography technology) Lauper et al., Oncogene 1998*
• IRef Biogrid Interaction: CCNE2 — CDK2 (direct interaction, pull down) Ramachandran et al., Science 2004
• IRef Biogrid Interaction: CCNE2 — CDK2 (direct interaction, two hybrid) Zariwala et al., Oncogene 1998
• IRef Biogrid Interaction: CCNE2 — CDK2 (physical association, affinity chromatography technology) Zariwala et al., Oncogene 1998
• IRef Hprd Interaction: CCNE2 — CDK2 (in vivo) Ramachandran et al., Science 2004, Gudas et al., Mol Cell Biol 1999*
• IRef Hprd Interaction: CCNE2 — CDK2 (in vitro) Ramachandran et al., Science 2004, Gudas et al., Mol Cell Biol 1999*
• IRef Intact Interaction: CCNE2 — CDK2 (direct interaction, inferred by curator) Hermjakob et al., Nucleic Acids Res 2004
• IRef Intact Interaction: CCNE2 — CDK2 (direct interaction, protein array) Ramachandran et al., Science 2004
• IRef Intact Interaction: CCNE2 — CDK2 (physical association, two hybrid) Zariwala et al., Oncogene 1998
• IRef Intact Interaction: CCNE2 — CDK2 (physical association, anti bait coimmunoprecipitation) Zariwala et al., Oncogene 1998
• IRef Intact Interaction: Complex of 18 proteins (association, tandem affinity purification) Varjosalo et al., Cell reports 2013
• IRef Intact Interaction: Complex of 30 proteins (association, tandem affinity purification) Varjosalo et al., Nat Methods 2013
• IRef Intact Interaction: Complex of 14 proteins (association, anti tag coimmunoprecipitation) Litovchick et al., Mol Cell 2007
• IRef Intact Interaction: Complex of 14 proteins (association, anti bait coimmunoprecipitation) Litovchick et al., Mol Cell 2007
• IRef Ophid Interaction: CCNE2 — CDK2 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Li et al., Hum Pathol 2001 (Adenocarcinoma...) : From the primary to the liver-metastatic foci, cyclin E apparently decreased, and CDK2 was reduced almost to zero
Zurlo et al., Mol Carcinog 2013 (Colonic Neoplasms...) : Consistently, cyclin D1, cyclin E , CDK2, and CDK4 proteins were reduced and histone H1-associated CDK2 kinase activity inhibited
Hartley et al., Dev Biol 1997 : To investigate the function of cyclin E during the early cycles, cyclin E/Cdk2 kinase activity was specifically inhibited in fertilized eggs by a truncated form of the Xenopus Cdk inhibitor, Xic1 ( Delta34Xic1 )