node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
asp-7 | gly-9 | F59D6.2.1 | Y47D3A.23a.1 | Peptidase A1 domain-containing protein; Belongs to the peptidase A1 family. | Probable N-acetylgalactosaminyltransferase 9; Probable glycopeptide transferase involved in O-linked oligosaccharide biosynthesis. Glycopeptide transferases catalyze the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide (By similarity). In contrast to other members of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. | 0.699 |
asp-7 | his-13 | F59D6.2.1 | ZK131.7.1 | Peptidase A1 domain-containing protein; Belongs to the peptidase A1 family. | Histone H3. | 0.666 |
gly-9 | asp-7 | Y47D3A.23a.1 | F59D6.2.1 | Probable N-acetylgalactosaminyltransferase 9; Probable glycopeptide transferase involved in O-linked oligosaccharide biosynthesis. Glycopeptide transferases catalyze the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide (By similarity). In contrast to other members of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. | Peptidase A1 domain-containing protein; Belongs to the peptidase A1 family. | 0.699 |
gly-9 | his-13 | Y47D3A.23a.1 | ZK131.7.1 | Probable N-acetylgalactosaminyltransferase 9; Probable glycopeptide transferase involved in O-linked oligosaccharide biosynthesis. Glycopeptide transferases catalyze the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide (By similarity). In contrast to other members of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. | Histone H3. | 0.461 |
his-13 | asp-7 | ZK131.7.1 | F59D6.2.1 | Histone H3. | Peptidase A1 domain-containing protein; Belongs to the peptidase A1 family. | 0.666 |
his-13 | gly-9 | ZK131.7.1 | Y47D3A.23a.1 | Histone H3. | Probable N-acetylgalactosaminyltransferase 9; Probable glycopeptide transferase involved in O-linked oligosaccharide biosynthesis. Glycopeptide transferases catalyze the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide (By similarity). In contrast to other members of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. | 0.461 |
his-13 | his-14 | ZK131.7.1 | ZK131.8.1 | Histone H3. | Histone H4. | 0.884 |
his-13 | his-45 | ZK131.7.1 | B0035.10.1 | Histone H3. | Histone H3; 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. | 0.801 |
his-13 | his-46 | ZK131.7.1 | B0035.9.1 | Histone H3. | 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. | 0.879 |
his-14 | his-13 | ZK131.8.1 | ZK131.7.1 | Histone H4. | Histone H3. | 0.884 |
his-14 | his-45 | ZK131.8.1 | B0035.10.1 | Histone H4. | Histone H3; 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. | 0.823 |
his-45 | his-13 | B0035.10.1 | ZK131.7.1 | Histone H3; 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 H3. | 0.801 |
his-45 | his-14 | B0035.10.1 | ZK131.8.1 | Histone H3; 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 H4. | 0.823 |
his-45 | his-46 | B0035.10.1 | B0035.9.1 | Histone H3; 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 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. | 0.957 |
his-46 | his-13 | B0035.9.1 | ZK131.7.1 | 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 H3. | 0.879 |
his-46 | his-45 | B0035.9.1 | B0035.10.1 | 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 H3; 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. | 0.957 |