• The 9-1-1 complex has also been found to interact with base excision repair factors human DNA polymerase beta, flap endonuclease FEN1, and the S. pombe MutY homolog (SpMYH), indicating that 9-1-1 also plays a direct role in DNA repair. (reactome.org)
  • RAD9A is highly similar to Schizosaccharomyces pombe rad9, a cell cycle checkpoint protein required for cell cycle arrest and DNA damage repair in response to DNA damage. (avivasysbio.com)
  • This complex is believed to be involved in cellular responses to DNA damage, possibly by associating with Rad17 and several components of the PCNA-loading heteropentamer, replication factor C. Human Rad1 exhibits significant homology to Rad1 from S. pombe, and its expression in yeast rad1 mutants has been shown to partially restore radiation resistance and G2 checkpoint activity. (biossusa.com)
  • HUS1 has been shown to interact with: HDAC1, PCNA, RAD1 homolog RAD17, and RAD9A. (wikipedia.org)
  • The Rad17-RFC and 9-1-1 complexes are structurally similar to the RFC (replication factor C) clamp loader and PCNA sliding clamp, respectively, and similar mechanisms are thought to be used during loading of the 9-1-1 complex and PCNA. (reactome.org)
  • Human Rad1 is a component of a heterotrimeric PCNA like complex that also contains the Rad9 and Hus1 proteins. (biossusa.com)
  • This protein forms a heterotrimeric complex with checkpoint proteins RAD9 and RAD1. (wikipedia.org)
  • The 9-1-1 complex is a heterotrimeric ring-shaped structure that is loaded onto DNA by the Rad17-RFC complex. (reactome.org)
  • It is not clear whether Rad1, Rad9 and Hus1 also have distinct functional activities independent of the heterotrimeric form. (biomedcentral.com)
  • In response to DNA damage, the trimeric complex interacts with another protein complex consisting of checkpoint protein RAD17 and four small subunits of the replication factor C (RFC), which loads the combined complex onto the chromatin. (wikipedia.org)
  • It forms a checkpoint protein complex with RAD1 and HUS1. (avivasysbio.com)
  • The Rad1 protein, evolutionarily conserved from yeast to humans, exists in cells as monomer as well as a component in the 9-1-1 protein complex. (biomedcentral.com)
  • The human mutY homolog (hMYH) is a base excision repair DNA glycosylase that excises adenines or 2-hydroxyadenines that are mispaired with guanine or 7,8-dihydro-8-oxoguanine (8-oxoG). (biomedcentral.com)
  • The purified Rad17 and Rad9-Hus1-Rad1 (9-1-1) complexes can form a stable co-complex in the presence of ATP, using Rad17-Rad9 interactions. (reactome.org)
  • During ATR signaling in response to DNA damage, Rad17 forms a complex with 9-1-1 and loads onto stalled replication forks [ 4 - 9 ]. (biomedcentral.com)
  • The S. cerevisiae checkpoint protein Rad17, the orthologue of human Rad1, forms a homocomplex in response to treatment with DNA damaging agents, and the complex is required for yeast survival after exposure to genotoxic agents [ 12 ]. (biomedcentral.com)
  • Checkpoint protein HUS1 is a protein that in humans is encoded by the HUS1 gene. (wikipedia.org)
  • To determine whether Rad1 functions to maintain genomic stability and prevent tumor development, we generated Mrad1 mutant mice by gene targeting. (biomedcentral.com)
  • From computer modeling studies, the Rad17 subunit of the complex is also proposed to interact with the C-terminus of Rad1, p36 with the C-terminus of Hus1, and p38 with the C-terminus of Rad9. (reactome.org)
  • In somatic cells the RAD9-RAD1-HUS1 (9-1-1) complex responds to DNA damage by promoting DNA repair. (wikipedia.org)
  • Moreover, we observed that hMYH was essential for the accumulation of hTopBP1 on damaged DNA, where hTopBP1 interacts with hRad9, a component of the Rad9-Hus1-Rad1 complex. (biomedcentral.com)
  • However, the presence of the 9-1-1 complex also alters the ability of Rad17 to become phosphorylated, perhaps suggesting that 9-1-1 may regulate the recruiment of additional ATR substrates. (reactome.org)
  • This complex is recruited by checkpoint protein RAD17 to the sites of DNA damage, which is thought to be important for triggering the checkpoint-signaling cascade. (avivasysbio.com)
  • These data suggest a possibility that Rad1 in humans and mice might have distinct functions independent of the 9-1-1 heterotrimer. (biomedcentral.com)
  • It is likely that increased Rad9 expression is needed for proliferation of tumor cells by mechanisms such as getting beyond (tolerating) oncogene-induced replicative stress and enhancing DNA repair capability. (biomedcentral.com)
  • Thus far, there has been no report addressing the function of Rad1 in carcinogenesis. (biomedcentral.com)
  • The 9-1-1 complex has also been found to interact with base excision repair factors human DNA polymerase beta, flap endonuclease FEN1, and the S. pombe MutY homolog (SpMYH), indicating that 9-1-1 also plays a direct role in DNA repair. (reactome.org)
  • 3. Physical and functional interactions between MutY glycosylase homologue (MYH) and checkpoint proteins Rad9-Rad1-Hus1. (nih.gov)
  • 4. A structural hinge in eukaryotic MutY homologues mediates catalytic activity and Rad9-Rad1-Hus1 checkpoint complex interactions. (nih.gov)
  • Genomic instability in disease and its fidelity in health depend on the DNA damage response (DDR), regulated in part from the complex of meiotic recombination 11 homolog 1 (MRE11), ATP-binding cassette-ATPase (RAD50), and phosphopeptide-binding Nijmegen breakage syndrome protein 1 (NBS1). (nih.gov)
  • In response to DNA damage, the trimeric complex interacts with another protein complex consisting of checkpoint protein RAD17 and four small subunits of the replication factor C (RFC), which loads the combined complex onto the chromatin. (wikipedia.org)
  • 2. SIRT6 protein deacetylase interacts with MYH DNA glycosylase, APE1 endonuclease, and Rad9-Rad1-Hus1 checkpoint clamp. (nih.gov)
  • 6. The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates NEIL1 glycosylase. (nih.gov)
  • 9. The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates DNA repair enzyme TDG glycosylase. (nih.gov)
  • Checkpoint protein HUS1 is a protein that in humans is encoded by the HUS1 gene. (wikipedia.org)
  • This protein forms a heterotrimeric complex with checkpoint proteins RAD9 and RAD1. (wikipedia.org)
  • 1. Association of the Rad9-Rad1-Hus1 checkpoint clamp with MYH DNA glycosylase and DNA. (nih.gov)
  • 7. An ordered assembly of MYH glycosylase, SIRT6 protein deacetylase, and Rad9-Rad1-Hus1 checkpoint clamp at oxidatively damaged telomeres. (nih.gov)
  • 8. The human checkpoint sensor and alternative DNA clamp Rad9-Rad1-Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery. (nih.gov)
  • 10. Repair activities of human 8-oxoguanine DNA glycosylase are stimulated by the interaction with human checkpoint sensor Rad9-Rad1-Hus1 complex. (nih.gov)
  • 13. Intramolecular Binding of the Rad9 C Terminus in the Checkpoint Clamp Rad9-Hus1-Rad1 Is Closely Linked with Its DNA Binding. (nih.gov)
  • 17. Crystal structure of the rad9-rad1-hus1 DNA damage checkpoint complex--implications for clamp loading and regulation. (nih.gov)
  • 19. Tri-cistronic cloning, overexpression and purification of human Rad9, Rad1, Hus1 protein complex. (nih.gov)
  • 11. Crystal structure of the human rad9-hus1-rad1 clamp. (nih.gov)
  • 14. Interaction between Rad9-Hus1-Rad1 and TopBP1 activates ATR-ATRIP and promotes TopBP1 recruitment to sites of UV-damage. (nih.gov)
  • 16. The effect of ionizing radiation on mRNA levels of the DNA damage response genes rad9, rad1 and hus1 in various mouse tissues. (nih.gov)