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PARP1 — PRKDC

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: PARP1 — PRKDC (physical association, affinity chromatography technology) Ju et al., Science 2006*
• MIPS CORUM NCOA6-DNA-PK-Ku-PARP1 complex: NCOA6-DNA-PK-Ku-PARP1 complex complex (NCOA6-PARP1-PRKDC-XRCC5-XRCC6) Ko et al., J Biol Chem 2003
• IRef Corum Interaction: Complex of NCOA6-PRKDC-XRCC5-XRCC6-PARP1 (association, pull down) Ko et al., J Biol Chem 2003
• IRef Dip Interaction: Complex of 21 proteins (tandem affinity purification) Shuaib et al., Proc Natl Acad Sci U S A 2010
• IRef Hprd Interaction: Complex of 51 proteins (in vivo) Rubin et al., Cancer Res 2007*
• IRef Hprd Interaction: Complex of 65 proteins Wong et al., Cell 2009
• IRef Hprd Interaction: Complex of 2739 proteins (in vivo) Czubaty et al., Biochim Biophys Acta 2005
• IRef Hprd Interaction: Complex of 50 proteins (in vivo) Mayeur et al., J Biol Chem 2005
• IRef Hprd Interaction: PARP1 — PRKDC (in vivo) Morrison et al., Nat Genet 1997*
• IRef Hprd Interaction: Complex of 37 proteins (in vivo) Ko et al., J Biol Chem 2003
• IRef Intact Interaction: Complex of 12 proteins (association, pull down) Kanno et al., EMBO J 2007
• IRef Intact Interaction: Complex of PARP1-ETS1-XRCC5-PRKDC-XRCC6 (association, anti tag coimmunoprecipitation) Brenner et al., Cancer Cell 2011
• IRef Intact Interaction: Complex of XRCC6-PARP1-XRCC5-PRKDC-ETV1 (association, anti tag coimmunoprecipitation) Brenner et al., Cancer Cell 2011
• IRef Intact Interaction: Complex of XRCC5-ERG-XRCC6-PARP1-PRKDC (association, anti tag coimmunoprecipitation) Brenner et al., Cancer Cell 2011
• IRef Intact Interaction: Complex of 46 proteins (association, anti tag coimmunoprecipitation) Abramson et al., Cell 2010
• IRef Intact Interaction: Complex of 117 proteins (association, tandem affinity purification) Zhao et al., Journal of proteomics 2011
• IRef Intact Interaction: Complex of 28 proteins (association, pull down) Czubaty et al., Biochim Biophys Acta 2005
• IRef Intact Interaction: Complex of 23 proteins (association, anti bait coimmunoprecipitation) Czubaty et al., Biochim Biophys Acta 2005
• IRef Intact Interaction: Complex of PRKDC-DDX5-SSRP1-PARP1-HDAC1-HDGF-SRSF1 (association, pull down) Zhao et al., Journal of proteomics 2011
• IRef Intact Interaction: Complex of 60 proteins (association, tandem affinity purification) Zhao et al., Journal of proteomics 2011
• IRef Intact Interaction: Complex of 306 proteins (association, pull down) Komarova et al., Mol Cell Proteomics 2011
• IRef Intact Interaction: Complex of 248 proteins (association, pull down) von Eyss et al., EMBO J 2012
• IRef Intact Interaction: Complex of 11 proteins (association, anti tag coimmunoprecipitation) Wong et al., Cell 2009
• IRef Intact Interaction: Complex of PRKDC-XRCC5-XRCC6-PARP1-XRCC6-PARP1-XRCC5-PRKDC (association, anti bait coimmunoprecipitation) Brenner et al., Cancer Cell 2011
• IRef Intact Interaction: Complex of XRCC6-PRKDC-XRCC5-PARP1-ERG (association, anti bait coimmunoprecipitation) Brenner et al., Cancer Cell 2011
• IRef Intact Interaction: Complex of 16 proteins (association, anti tag coimmunoprecipitation) Abramson et al., Cell 2010
• IRef Intact Interaction: Complex of XRCC6-PARP1-PRKDC (association, anti bait coimmunoprecipitation) Brenner et al., Cancer Cell 2011
• IRef Intact Interaction: Complex of PARP1-PRKDC-XRCC5-XRCC6-SPI1 (association, anti tag coimmunoprecipitation) Brenner et al., Cancer Cell 2011
• IRef Intact Interaction: Complex of TOP2B-PRKDC-USF1-KAT2B-PARP1-XRCC5 (physical association, anti bait coimmunoprecipitation) Wong et al., Cell 2009
• IRef Intact Interaction: Complex of PARP1-PRKDC-TOP2A-XRCC5 (association, anti bait coimmunoprecipitation) Abramson et al., Cell 2010
• IRef Intact Interaction: Complex of PRKDC-ERG-PARP1-ERG-PRKDC-PARP1 (association, anti bait coimmunoprecipitation) Brenner et al., Cancer Cell 2011
• IRef Intact Interaction: Complex of H2AFX-XRCC5-TOP2A-AIRE-PARP1-PRKDC (association, anti bait coimmunoprecipitation) Abramson et al., Cell 2010
• IRef Intact Interaction: Complex of 21 proteins (physical association, anti tag coimmunoprecipitation) Behrends et al., Nature 2010
• IRef Intact Interaction: Complex of TOP2B-HDAC9-PRKDC-XRCC5-USF1-PARP1-XRCC6-KAT2B-USF2 (association, anti bait coimmunoprecipitation) Wong et al., Cell 2009
• IRef Intact Interaction: Complex of ERG-PARP1-PRKDC-XRCC5 (association, anti bait coimmunoprecipitation) Brenner et al., Cancer Cell 2011
• IRef Ophid Interaction: PARP1 — PRKDC (aggregation, confirmational text mining) Morrison et al., Nat Genet 1997*
• IRef Ophid Interaction: PARP1 — PRKDC (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Ariumi et al., Oncogene 1999 : Thus, DNA-PK suppresses PARP activity, probably through direct binding and/or sequestration of DNA-ends which serve as an important stimulator for both enzymes
Veuger et al., Oncogene 2004 : Inactive DNA-PK suppressed the activity of PARP-1 and vice versa ... The inhibitory effect of DNA-PK on PARP activity was confirmed in permeabilized cells
Dregalla et al., Aging 2010 (Chromosomal Instability...) : We provide the first evidence for regulation of DNA-PKcs by tankyrase 1 PARP activity and taken together, identify roles of tankyrase 1 with implications not only for DNA repair and telomere biology, but also for cancer and aging
Calkins et al., Nucleic Acids Res 2013 : Loss of DNA-PK function prevented activation of PARP-1 and its recruitment to chromatin in damaged cells, suggesting regulation of PARP-1 by DNA-PK within a pathway of DNA repair
Ruscetti et al., J Biol Chem 1998 : The protein kinase activity of DNA-PK can be stimulated by PARP in the presence of NAD+ in a reaction that is blocked by the PARP inhibitor 1, 5-dihydroxyisoquinoline