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BLM — RMI2

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

Studies that report less than 10 interactions are marked with *

• IRef Dip Interaction: RMI2 — BLM (physical association, anti tag coimmunoprecipitation) Hoadley et al., Structure 2010*
• IRef Dip Interaction: RMI2 — BLM (physical association, anti tag coimmunoprecipitation) Wang et al., Structure 2010*
• IRef Dip Interaction: Complex of 13 proteins (anti tag coimmunoprecipitation) Hoadley et al., Structure 2010*
• IRef Intact Interaction: Complex of KPNB1-RPA2-SSBP1-RMI2-BLM (physical association, tandem affinity purification) Hutchins et al., Science 2010
• IRef Intact Interaction: Complex of BLM-RMI1-SSBP1-PLK1-RMI2-ERCC6L (physical association, tandem affinity purification) Hutchins et al., Science 2010
• IRef Intact Interaction: Complex of 21 proteins (association, anti bait coimmunoprecipitation) Xu et al., EMBO J 2010
• IRef Intact Interaction: Complex of RMI1-BLM-TOP3A-RPA3-RIF1-POLR1A-RMI2-POLR1B (association, anti bait coimmunoprecipitation) Xu et al., EMBO J 2010
• IRef Intact Interaction: Complex of RMI1-RPA3-BLM-RPA2-PGAM5-SSBP1-NDUFAF7-RMI2 (physical association, tandem affinity purification) Hutchins et al., Science 2010

Text-mined interactions from Literome

Xu et al., Genes Dev 2008 (Bloom Syndrome...) : Nevertheless, RMI stimulates the dissolution of a homologous recombination intermediate in vitro and is essential for the stability, localization, and function of the BLM complex in vivo
Singh et al., Genes Dev 2008 (Bloom Syndrome...) : Fourth, BLAP18/RMI2 is required to target BLM to chromatin and for the assembly of BLM foci upon hydroxyurea treatment