PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29281621-3 2017 In eukaryotes, Rad6- and Rad18-mediated PCNA ubiquitination at lysine 164 promotes recruitment of TLS polymerases, allowing cells to efficiently cope with DNA damage. Lysine 63-69 E3 ubiquitin-protein ligase RAD18 Saccharomyces cerevisiae S288C 25-30 18824138-1 2009 The Rad6-Rad18 complex mono-ubiquitinates proliferating cell nuclear antigen (PCNA) at the lysine 164 residue after DNA damage and promotes DNA polymerase eta (Poleta)- and Polzeta/Rev1-dependent DNA synthesis. Lysine 91-97 E3 ubiquitin-protein ligase RAD18 Saccharomyces cerevisiae S288C 9-14 17709386-1 2007 Treatment of Saccharomyces cerevisiae cells with DNA-damaging agents elicits lysine 164-linked PCNA monoubiquitination by Rad6-Rad18. Lysine 77-83 E3 ubiquitin-protein ligase RAD18 Saccharomyces cerevisiae S288C 127-132 16783012-4 2006 This substitution appears to abolish all DNA damage-tolerance activities normally carried out by the RAD6/RAD18 pathway, including translesion replication by DNA polymerase zeta/Rev1 and DNA polymerase eta, and the error-free, recombination-dependent component of this pathway, but has little effect on the growth rate, suggesting that G178S may prevent ubiquitination of lysine 164 in PCNA. Lysine 372-378 E3 ubiquitin-protein ligase RAD18 Saccharomyces cerevisiae S288C 106-111 16344468-1 2005 In response to DNA damage, the Rad6/Rad18 ubiquitin-conjugating complex monoubiquitinates the replication clamp proliferating cell nuclear antigen (PCNA) at Lys-164. Lysine 157-160 E3 ubiquitin-protein ligase RAD18 Saccharomyces cerevisiae S288C 36-41 15121847-3 2004 It has been shown recently that following treatment of yeast cells with DNA-damaging agents, the lysine 164 residue of PCNA becomes monoubiquitinated in a Rad6-Rad18-dependent manner and that subsequently this PCNA residue is polyubiquitinated via a lysine 63-linked ubiquitin chain in an Mms2-Ubc13-, Rad5-dependent manner. Lysine 97-103 E3 ubiquitin-protein ligase RAD18 Saccharomyces cerevisiae S288C 160-165