| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Abd-B | His3.3A | FBpp0373669 | FBpp0305716 | Homeobox protein abdominal-B; Abdominal B (Abd-B) is one of the three hox genes of the bithorax complex. The product of Abd-B specifies the identity of the posterior abdominal segments, the external genitalia and the gonads. It is also involved in regulating the post-mating-response. | Histone H3.3A; Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. 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 mach [...] | 0.459 |
| Abd-B | His3:CG31613 | FBpp0373669 | FBpp0085250 | Homeobox protein abdominal-B; Abdominal B (Abd-B) is one of the three hox genes of the bithorax complex. The product of Abd-B specifies the identity of the posterior abdominal segments, the external genitalia and the gonads. It is also involved in regulating the post-mating-response. | 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. | 0.467 |
| Abd-B | Ho | FBpp0373669 | FBpp0081900 | Homeobox protein abdominal-B; Abdominal B (Abd-B) is one of the three hox genes of the bithorax complex. The product of Abd-B specifies the identity of the posterior abdominal segments, the external genitalia and the gonads. It is also involved in regulating the post-mating-response. | Heme oxygenase; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. | 0.836 |
| Abd-B | Pc | FBpp0373669 | FBpp0078059 | Homeobox protein abdominal-B; Abdominal B (Abd-B) is one of the three hox genes of the bithorax complex. The product of Abd-B specifies the identity of the posterior abdominal segments, the external genitalia and the gonads. It is also involved in regulating the post-mating-response. | Polycomb group protein Pc; Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Component of the PcG multiprotein PRC1 complex, a complex that acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-118', rendering chromatin heritably changed in its expressibility. Promotes locus-specif [...] | 0.708 |
| CG5037 | Cchl | FBpp0079582 | FBpp0083583 | Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O. Belongs to the ubiA prenyltransferase family. | Cytochrome c heme lyase; Links covalently the heme group to the apoprotein of cytochrome c. | 0.993 |
| CG5037 | FeCH | FBpp0079582 | FBpp0085208 | Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O. Belongs to the ubiA prenyltransferase family. | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.950 |
| CG5037 | Ho | FBpp0079582 | FBpp0081900 | Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O. Belongs to the ubiA prenyltransferase family. | Heme oxygenase; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. | 0.908 |
| Cchl | CG5037 | FBpp0083583 | FBpp0079582 | Cytochrome c heme lyase; Links covalently the heme group to the apoprotein of cytochrome c. | Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O. Belongs to the ubiA prenyltransferase family. | 0.993 |
| Cchl | FeCH | FBpp0083583 | FBpp0085208 | Cytochrome c heme lyase; Links covalently the heme group to the apoprotein of cytochrome c. | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.913 |
| Cchl | Ho | FBpp0083583 | FBpp0081900 | Cytochrome c heme lyase; Links covalently the heme group to the apoprotein of cytochrome c. | Heme oxygenase; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. | 0.909 |
| Cchl | fh | FBpp0083583 | FBpp0071283 | Cytochrome c heme lyase; Links covalently the heme group to the apoprotein of cytochrome c. | Frataxin homolog, mitochondrial; Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+). May be able to store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization. Required for ecdysteroidogenesis in the prothoracic gland which is necessary for larval to pupal transition. Belongs to the frataxin family. | 0.475 |
| Cpr | Ho | FBpp0078880 | FBpp0081900 | NADPH--cytochrome P450 reductase; This enzyme is required for electron transfer from NADP to cytochrome p450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome b5 (By similarity). May function to clear the olfactory organ (antennae) from accumulating chemicals. In the N-terminal section; belongs to the flavodoxin family. | Heme oxygenase; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. | 0.832 |
| FeCH | CG5037 | FBpp0085208 | FBpp0079582 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O. Belongs to the ubiA prenyltransferase family. | 0.950 |
| FeCH | Cchl | FBpp0085208 | FBpp0083583 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | Cytochrome c heme lyase; Links covalently the heme group to the apoprotein of cytochrome c. | 0.913 |
| FeCH | Ho | FBpp0085208 | FBpp0081900 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | Heme oxygenase; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. | 0.950 |
| FeCH | fh | FBpp0085208 | FBpp0071283 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | Frataxin homolog, mitochondrial; Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+). May be able to store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization. Required for ecdysteroidogenesis in the prothoracic gland which is necessary for larval to pupal transition. Belongs to the frataxin family. | 0.969 |
| His3.3A | Abd-B | FBpp0305716 | FBpp0373669 | Histone H3.3A; Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. 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 mach [...] | Homeobox protein abdominal-B; Abdominal B (Abd-B) is one of the three hox genes of the bithorax complex. The product of Abd-B specifies the identity of the posterior abdominal segments, the external genitalia and the gonads. It is also involved in regulating the post-mating-response. | 0.459 |
| His3.3A | His3:CG31613 | FBpp0305716 | FBpp0085250 | Histone H3.3A; Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. 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 mach [...] | 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. | 0.958 |
| His3.3A | Ho | FBpp0305716 | FBpp0081900 | Histone H3.3A; Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. 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 mach [...] | Heme oxygenase; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. | 0.842 |
| His3.3A | Pc | FBpp0305716 | FBpp0078059 | Histone H3.3A; Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. 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 mach [...] | Polycomb group protein Pc; Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Component of the PcG multiprotein PRC1 complex, a complex that acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-118', rendering chromatin heritably changed in its expressibility. Promotes locus-specif [...] | 0.995 |