node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
C7M84_012868 | C7M84_013020 | A0A3R7Q5C5 | A0A423SXA4 | 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. | Putative E3 ubiquitin-protein ligase HERC1 isoform X3. | 0.425 |
C7M84_012868 | C7M84_013021 | A0A3R7Q5C5 | A0A423SX34 | 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. | 0.425 |
C7M84_012868 | C7M84_013022 | A0A3R7Q5C5 | A0A3R7NWN7 | 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. | Putative E3 ubiquitin-protein ligase HERC1 isoform X4. | 0.425 |
C7M84_012868 | C7M84_013024 | A0A3R7Q5C5 | A0A423SXG1 | 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. | 0.425 |
C7M84_012868 | C7M84_013025 | A0A3R7Q5C5 | A0A423SX54 | 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. | Putative E3 ubiquitin-protein ligase HERC1. | 0.425 |
C7M84_012868 | C7M84_013027 | A0A3R7Q5C5 | A0A3R7PJR4 | 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. | Putative E3 ubiquitin-protein ligase HERC1. | 0.425 |
C7M84_012868 | C7M84_013028 | A0A3R7Q5C5 | A0A423SX96 | 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. | Putative E3 ubiquitin-protein ligase HERC1 isoform X1. | 0.425 |
C7M84_012868 | C7M84_017462 | A0A3R7Q5C5 | A0A3R7NRA9 | 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. | Putative E3 ubiquitin-protein ligase HERC2 isoform X1. | 0.425 |
C7M84_012868 | C7M84_023340 | A0A3R7Q5C5 | A0A3R7MJM5 | 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. | AN1-type zinc finger and ubiquitin domain-containing protein 1. | 0.617 |
C7M84_013020 | C7M84_012868 | A0A423SXA4 | A0A3R7Q5C5 | Putative E3 ubiquitin-protein ligase HERC1 isoform X3. | 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. | 0.425 |
C7M84_013020 | C7M84_013022 | A0A423SXA4 | A0A3R7NWN7 | Putative E3 ubiquitin-protein ligase HERC1 isoform X3. | Putative E3 ubiquitin-protein ligase HERC1 isoform X4. | 0.870 |
C7M84_013020 | C7M84_017462 | A0A423SXA4 | A0A3R7NRA9 | Putative E3 ubiquitin-protein ligase HERC1 isoform X3. | Putative E3 ubiquitin-protein ligase HERC2 isoform X1. | 0.899 |
C7M84_013020 | C7M84_023340 | A0A423SXA4 | A0A3R7MJM5 | Putative E3 ubiquitin-protein ligase HERC1 isoform X3. | AN1-type zinc finger and ubiquitin domain-containing protein 1. | 0.432 |
C7M84_013021 | C7M84_012868 | A0A423SX34 | A0A3R7Q5C5 | 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. | 0.425 |
C7M84_013021 | C7M84_013022 | A0A423SX34 | A0A3R7NWN7 | Uncharacterized protein. | Putative E3 ubiquitin-protein ligase HERC1 isoform X4. | 0.466 |
C7M84_013021 | C7M84_023340 | A0A423SX34 | A0A3R7MJM5 | Uncharacterized protein. | AN1-type zinc finger and ubiquitin domain-containing protein 1. | 0.432 |
C7M84_013022 | C7M84_012868 | A0A3R7NWN7 | A0A3R7Q5C5 | Putative E3 ubiquitin-protein ligase HERC1 isoform X4. | 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. | 0.425 |
C7M84_013022 | C7M84_013020 | A0A3R7NWN7 | A0A423SXA4 | Putative E3 ubiquitin-protein ligase HERC1 isoform X4. | Putative E3 ubiquitin-protein ligase HERC1 isoform X3. | 0.870 |
C7M84_013022 | C7M84_013021 | A0A3R7NWN7 | A0A423SX34 | Putative E3 ubiquitin-protein ligase HERC1 isoform X4. | Uncharacterized protein. | 0.466 |
C7M84_013022 | C7M84_013024 | A0A3R7NWN7 | A0A423SXG1 | Putative E3 ubiquitin-protein ligase HERC1 isoform X4. | Uncharacterized protein. | 0.496 |