| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAMKMT | H3-2 | ENSP00000367755 | ENSP00000499501 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | H3.2 histone. | 0.662 |
| CAMKMT | H3-3B | ENSP00000367755 | ENSP00000254810 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | Histone H3.3; Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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 [...] | 0.662 |
| CAMKMT | H3-4 | ENSP00000367755 | ENSP00000355657 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | Histone H3.1t; 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. | 0.662 |
| CAMKMT | H3-5 | ENSP00000367755 | ENSP00000339835 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | Histone H3.3C; 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. Hominid-specific H3.5/H3F3C preferentially colocalizes with euchromatin, and it is associated with actively transcribed genes. | 0.662 |
| CAMKMT | H3C12 | ENSP00000367755 | ENSP00000352252 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | Histone H3.1; 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. | 0.662 |
| CAMKMT | H3C13 | ENSP00000367755 | ENSP00000333277 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | Histone H3.2; 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. | 0.662 |
| CAMKMT | PRDM7 | ENSP00000367755 | ENSP00000496449 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | Probable histone-lysine N-methyltransferase PRDM7; Probable histone methyltransferase. | 0.675 |
| CAMKMT | PRDM9 | ENSP00000367755 | ENSP00000296682 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | Histone-lysine N-methyltransferase PRDM9; Histone methyltransferase that sequentially mono-, di-, and tri-methylates both 'Lys-4' (H3K4) and 'Lys-36' (H3K36) of histone H3 to produce respectively trimethylated 'Lys-4' (H3K4me3) and trimethylated 'Lys-36' (H3K36me3) histone H3 and plays a key role in meiotic prophase by determining hotspot localization thereby promoting meiotic recombination. Also can methylate all four core histones with H3 being the best substrate and the most highly modified. Is also able, on one hand, to mono and di-methylate H4K20 and on other hand to trimethylate [...] | 0.744 |
| H2AX | H3-2 | ENSP00000434024 | ENSP00000499501 | Histone H2AX; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low dos [...] | H3.2 histone. | 0.985 |
| H2AX | H3-3B | ENSP00000434024 | ENSP00000254810 | Histone H2AX; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low dos [...] | Histone H3.3; Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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 [...] | 0.996 |
| H2AX | H3-4 | ENSP00000434024 | ENSP00000355657 | Histone H2AX; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low dos [...] | Histone H3.1t; 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. | 0.995 |
| H2AX | H3-5 | ENSP00000434024 | ENSP00000339835 | Histone H2AX; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low dos [...] | Histone H3.3C; 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. Hominid-specific H3.5/H3F3C preferentially colocalizes with euchromatin, and it is associated with actively transcribed genes. | 0.985 |
| H2AX | H3C12 | ENSP00000434024 | ENSP00000352252 | Histone H2AX; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low dos [...] | Histone H3.1; 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. | 0.985 |
| H2AX | H3C13 | ENSP00000434024 | ENSP00000333277 | Histone H2AX; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low dos [...] | Histone H3.2; 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. | 0.990 |
| H2AX | PRDM9 | ENSP00000434024 | ENSP00000296682 | Histone H2AX; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low dos [...] | Histone-lysine N-methyltransferase PRDM9; Histone methyltransferase that sequentially mono-, di-, and tri-methylates both 'Lys-4' (H3K4) and 'Lys-36' (H3K36) of histone H3 to produce respectively trimethylated 'Lys-4' (H3K4me3) and trimethylated 'Lys-36' (H3K36me3) histone H3 and plays a key role in meiotic prophase by determining hotspot localization thereby promoting meiotic recombination. Also can methylate all four core histones with H3 being the best substrate and the most highly modified. Is also able, on one hand, to mono and di-methylate H4K20 and on other hand to trimethylate [...] | 0.733 |
| H2AX | SPO11 | ENSP00000434024 | ENSP00000360310 | Histone H2AX; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low dos [...] | Meiotic recombination protein SPO11; Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with TOP6BL, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles. Essential for the phosphorylation of SMC3, HORMAD1 and HORMAD2. | 0.687 |
| H3-2 | CAMKMT | ENSP00000499501 | ENSP00000367755 | H3.2 histone. | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | 0.662 |
| H3-2 | H2AX | ENSP00000499501 | ENSP00000434024 | H3.2 histone. | Histone H2AX; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low dos [...] | 0.985 |
| H3-2 | H3-3B | ENSP00000499501 | ENSP00000254810 | H3.2 histone. | Histone H3.3; Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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 [...] | 0.955 |
| H3-2 | H3-4 | ENSP00000499501 | ENSP00000355657 | H3.2 histone. | Histone H3.1t; 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. | 0.997 |