node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AdSL | Asph | FBpp0082816 | FBpp0307715 | Adenylosuccinate Lyase (AdSL) encodes a protein that might be a lyase involved in purine nucleotide metabolic process based on orthology; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily. | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | 0.626 |
AdSL | CG3021 | FBpp0082816 | FBpp0070168 | Adenylosuccinate Lyase (AdSL) encodes a protein that might be a lyase involved in purine nucleotide metabolic process based on orthology; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily. | Mitochondrial tRNA-specific 2-thiouridylase 1; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base. Belongs to the MnmA/TRMU family. | 0.727 |
Asph | AdSL | FBpp0307715 | FBpp0082816 | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | Adenylosuccinate Lyase (AdSL) encodes a protein that might be a lyase involved in purine nucleotide metabolic process based on orthology; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily. | 0.626 |
Asph | CG10465 | FBpp0307715 | FBpp0085430 | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | RE57120p; It is involved in the biological process described with: protein homooligomerization. | 0.573 |
Asph | CG3021 | FBpp0307715 | FBpp0070168 | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | Mitochondrial tRNA-specific 2-thiouridylase 1; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base. Belongs to the MnmA/TRMU family. | 0.602 |
Asph | His3.3A | FBpp0307715 | FBpp0305716 | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | 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 [...] | 0.691 |
Asph | His3:CG31613 | FBpp0307715 | FBpp0085250 | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | 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. | 0.691 |
Asph | MTA1-like | FBpp0307715 | FBpp0303347 | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | Metastasis associated 1-like, isoform D; It is involved in the biological process described with: chromosome condensation; negative regulation of transcription by RNA polymerase II; heterochromatin organization involved in chromatin silencing; histone deacetylation. | 0.619 |
Asph | Orc1 | FBpp0307715 | FBpp0088033 | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | Origin recognition complex subunit 1 (Orc1) encodes the largest subunit of the origin recognition complex (ORC), which is essential for the initiation of DNA replication in eukaryotic cells. The ATPase activity of the product of Orc1 is critical for the formation and function of the pre-replicative complex. The regulated degradation of the product of Orc1 by ubiquitin-mediated proteolysis after initiation of DNA replication helps to prevent re-replication. | 0.615 |
Asph | Orc3 | FBpp0307715 | FBpp0086881 | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | Origin recognition complex subunit 3 (Orc3) encodes a subunit of the origin recognition complex. It is involved in DNA replication initiation and border follicle cell migration regulation. | 0.617 |
Asph | Orc6 | FBpp0307715 | FBpp0087566 | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | Origin recognition complex subunit 6; Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity). | 0.664 |
Asph | sicily | FBpp0307715 | FBpp0311993 | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | NADH dehydrogenase (ubiquinone) complex I, assembly factor 6 homolog; Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) at early stages; Belongs to the NDUFAF6 family. | 0.641 |
CG10465 | Asph | FBpp0085430 | FBpp0307715 | RE57120p; It is involved in the biological process described with: protein homooligomerization. | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | 0.573 |
CG3021 | AdSL | FBpp0070168 | FBpp0082816 | Mitochondrial tRNA-specific 2-thiouridylase 1; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base. Belongs to the MnmA/TRMU family. | Adenylosuccinate Lyase (AdSL) encodes a protein that might be a lyase involved in purine nucleotide metabolic process based on orthology; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily. | 0.727 |
CG3021 | Asph | FBpp0070168 | FBpp0307715 | Mitochondrial tRNA-specific 2-thiouridylase 1; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base. Belongs to the MnmA/TRMU family. | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | 0.602 |
His3.3A | Asph | FBpp0305716 | FBpp0307715 | 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 [...] | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | 0.691 |
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 | MTA1-like | FBpp0305716 | FBpp0303347 | 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 [...] | Metastasis associated 1-like, isoform D; It is involved in the biological process described with: chromosome condensation; negative regulation of transcription by RNA polymerase II; heterochromatin organization involved in chromatin silencing; histone deacetylation. | 0.600 |
His3:CG31613 | Asph | FBpp0085250 | FBpp0307715 | 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. | Aspartyl beta-hydroxylase (Asph) may be involved in peptidyl-amino acid modification based on orthology. It might be involved in neurogenesis since lack of Asph function enhances the expanded htt-fragment-induced eye phenotype. | 0.691 |
His3:CG31613 | His3.3A | FBpp0085250 | FBpp0305716 | 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 H3.3A; 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 [...] | 0.958 |