node1 | node2 | node1 annotation | node2 annotation | score |
A0A2T6ZCD5 | A0A2T6ZIY9 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. | 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. | 0.977 |
A0A2T6ZCD5 | A0A2T6ZIZ6 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. | Uncharacterized protein; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily. | 0.976 |
A0A2T6ZCD5 | A0A2T6ZLQ4 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. | Uncharacterized protein. | 0.941 |
A0A2T6ZCD5 | A0A2T6ZM74 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. | 0.975 |
A0A2T6ZCD5 | A0A2T6ZML8 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. | Beta centromeric histone H3. | 0.947 |
A0A2T6ZCD5 | A0A2T6ZPA0 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. | SET domain-containing protein. | 0.935 |
A0A2T6ZCD5 | A0A2T6ZRR1 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. | Histone-fold-containing protein. | 0.947 |
A0A2T6ZCD5 | A0A2T6ZWU2 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. | Histone-fold-containing protein. | 0.947 |
A0A2T6ZCD5 | A0A2T6ZZU0 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. | Uncharacterized protein. | 0.889 |
A0A2T6ZCD5 | A0A2T7A4X7 | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. | Uncharacterized protein. | 0.912 |
A0A2T6ZIY9 | A0A2T6ZCD5 | 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. | Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. | 0.977 |
A0A2T6ZIY9 | A0A2T6ZIZ6 | 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; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily. | 0.973 |
A0A2T6ZIY9 | A0A2T6ZLQ4 | 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. | 0.810 |
A0A2T6ZIY9 | A0A2T6ZM74 | 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. | Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. | 0.954 |
A0A2T6ZIY9 | A0A2T6ZML8 | 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. | Beta centromeric histone H3. | 0.968 |
A0A2T6ZIY9 | A0A2T6ZPA0 | 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. | SET domain-containing protein. | 0.913 |
A0A2T6ZIY9 | A0A2T6ZRR1 | 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. | Histone-fold-containing protein. | 0.968 |
A0A2T6ZIY9 | A0A2T6ZWU2 | 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. | Histone-fold-containing protein. | 0.968 |
A0A2T6ZIY9 | A0A2T6ZZU0 | 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. | 0.755 |
A0A2T6ZIY9 | A0A2T7A4X7 | 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. | 0.744 |