node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
B3RJ01_TRIAD | B3RUM8_TRIAD | B3RJ01 | B3RUM8 | Uncharacterized protein. | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | 0.982 |
B3RJ01_TRIAD | B3RV95_TRIAD | B3RJ01 | B3RV95 | Uncharacterized protein. | RPOLD domain-containing protein. | 0.987 |
B3RJ01_TRIAD | B3S4B9_TRIAD | B3RJ01 | B3S4B9 | Uncharacterized protein. | FACT complex subunit SSRP1; Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment o [...] | 0.999 |
B3RJ01_TRIAD | B3S7D7_TRIAD | B3RJ01 | B3S7D7 | Uncharacterized protein. | Uncharacterized protein. | 0.786 |
B3RJ01_TRIAD | B3SAD9_TRIAD | B3RJ01 | B3SAD9 | Uncharacterized protein. | Plus3 domain-containing protein. | 0.978 |
B3RJ01_TRIAD | B3SBS3_TRIAD | B3RJ01 | B3SBS3 | Uncharacterized protein. | Uncharacterized protein. | 0.996 |
B3RR98_TRIAD | B3S7D7_TRIAD | B3RR98 | B3S7D7 | Uncharacterized protein. | Uncharacterized protein. | 0.690 |
B3RUM8_TRIAD | B3RJ01_TRIAD | B3RUM8 | B3RJ01 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Uncharacterized protein. | 0.982 |
B3RUM8_TRIAD | B3RV95_TRIAD | B3RUM8 | B3RV95 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | RPOLD domain-containing protein. | 0.943 |
B3RUM8_TRIAD | B3S0B0_TRIAD | B3RUM8 | B3S0B0 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | CHDCT2 domain-containing protein. | 0.432 |
B3RUM8_TRIAD | B3S0E8_TRIAD | B3RUM8 | B3S0E8 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | ARID domain-containing protein. | 0.997 |
B3RUM8_TRIAD | B3S4B9_TRIAD | B3RUM8 | B3S4B9 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | FACT complex subunit SSRP1; Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment o [...] | 0.980 |
B3RUM8_TRIAD | B3S7D7_TRIAD | B3RUM8 | B3S7D7 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Uncharacterized protein. | 0.760 |
B3RUM8_TRIAD | B3SAD9_TRIAD | B3RUM8 | B3SAD9 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Plus3 domain-containing protein. | 0.788 |
B3RUM8_TRIAD | B3SBS3_TRIAD | B3RUM8 | B3SBS3 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Uncharacterized protein. | 0.868 |
B3RV95_TRIAD | B3RJ01_TRIAD | B3RV95 | B3RJ01 | RPOLD domain-containing protein. | Uncharacterized protein. | 0.987 |
B3RV95_TRIAD | B3RUM8_TRIAD | B3RV95 | B3RUM8 | RPOLD domain-containing protein. | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | 0.943 |
B3RV95_TRIAD | B3S0E8_TRIAD | B3RV95 | B3S0E8 | RPOLD domain-containing protein. | ARID domain-containing protein. | 0.478 |
B3RV95_TRIAD | B3S4B9_TRIAD | B3RV95 | B3S4B9 | RPOLD domain-containing protein. | FACT complex subunit SSRP1; Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment o [...] | 0.962 |
B3RV95_TRIAD | B3S7D7_TRIAD | B3RV95 | B3S7D7 | RPOLD domain-containing protein. | Uncharacterized protein. | 0.705 |