| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AIFM1 | CR201_G0017591 | ENSPPYP00000023188 | ENSPPYP00000017667 | AIFM1 isoform 7. | Core histone macro-H2A; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. | 0.685 |
| AIFM1 | H2AZ1 | ENSPPYP00000023188 | ENSPPYP00000016702 | AIFM1 isoform 7. | Histone H2A.Z; 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. May be involved in the formation of constitutive heterochromatin. May be required for c [...] | 0.650 |
| AIFM1 | LOC100446892 | ENSPPYP00000023188 | ENSPPYP00000006743 | AIFM1 isoform 7. | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.858 |
| AIFM1 | MACROH2A2 | ENSPPYP00000023188 | ENSPPYP00000002759 | AIFM1 isoform 7. | Core histone macro-H2A; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. | 0.685 |
| BSG | LOC100446892 | ENSPPYP00000010416 | ENSPPYP00000006743 | BSG isoform 4. | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.795 |
| CR201_G0017591 | AIFM1 | ENSPPYP00000017667 | ENSPPYP00000023188 | Core histone macro-H2A; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. | AIFM1 isoform 7. | 0.685 |
| CR201_G0017591 | H2AZ1 | ENSPPYP00000017667 | ENSPPYP00000016702 | Core histone macro-H2A; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. | Histone H2A.Z; 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. May be involved in the formation of constitutive heterochromatin. May be required for c [...] | 0.616 |
| CR201_G0017591 | LOC100446892 | ENSPPYP00000017667 | ENSPPYP00000006743 | Core histone macro-H2A; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.699 |
| CR201_G0017591 | MACROH2A2 | ENSPPYP00000017667 | ENSPPYP00000002759 | Core histone macro-H2A; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. | Core histone macro-H2A; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. | 0.904 |
| H2AZ1 | AIFM1 | ENSPPYP00000016702 | ENSPPYP00000023188 | Histone H2A.Z; 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. May be involved in the formation of constitutive heterochromatin. May be required for c [...] | AIFM1 isoform 7. | 0.650 |
| H2AZ1 | CR201_G0017591 | ENSPPYP00000016702 | ENSPPYP00000017667 | Histone H2A.Z; 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. May be involved in the formation of constitutive heterochromatin. May be required for c [...] | Core histone macro-H2A; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. | 0.616 |
| H2AZ1 | LOC100446892 | ENSPPYP00000016702 | ENSPPYP00000006743 | Histone H2A.Z; 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. May be involved in the formation of constitutive heterochromatin. May be required for c [...] | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.694 |
| H2AZ1 | MACROH2A2 | ENSPPYP00000016702 | ENSPPYP00000002759 | Histone H2A.Z; 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. May be involved in the formation of constitutive heterochromatin. May be required for c [...] | Core histone macro-H2A; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. | 0.616 |
| LOC100446892 | AIFM1 | ENSPPYP00000006743 | ENSPPYP00000023188 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | AIFM1 isoform 7. | 0.858 |
| LOC100446892 | BSG | ENSPPYP00000006743 | ENSPPYP00000010416 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | BSG isoform 4. | 0.795 |
| LOC100446892 | CR201_G0017591 | ENSPPYP00000006743 | ENSPPYP00000017667 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Core histone macro-H2A; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. | 0.699 |
| LOC100446892 | H2AZ1 | ENSPPYP00000006743 | ENSPPYP00000016702 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Histone H2A.Z; 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. May be involved in the formation of constitutive heterochromatin. May be required for c [...] | 0.694 |
| LOC100446892 | MACROH2A2 | ENSPPYP00000006743 | ENSPPYP00000002759 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Core histone macro-H2A; Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. | 0.699 |
| LOC100446892 | RPL14 | ENSPPYP00000006743 | ENSPPYP00000023762 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | RPL14 isoform 1. | 0.696 |
| LOC100446892 | RPL23 | ENSPPYP00000006743 | ENSPPYP00000009553 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 60S ribosomal protein L23; Belongs to the universal ribosomal protein uL14 family. | 0.760 |
