| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACD | ADPRH | ENSP00000483117 | ENSP00000420200 | Adrenocortical dysplasia protein homolog; Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends. Without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Promotes binding of POT1 to single-stranded telomeric DNA. Modulates the inhibitory effects of POT1 on telomere elongation. The ACD-POT1 heterodim [...] | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | 0.415 |
| ADPRH | ACD | ENSP00000420200 | ENSP00000483117 | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | Adrenocortical dysplasia protein homolog; Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends. Without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Promotes binding of POT1 to single-stranded telomeric DNA. Modulates the inhibitory effects of POT1 on telomere elongation. The ACD-POT1 heterodim [...] | 0.415 |
| ADPRH | ADPRHL2 | ENSP00000420200 | ENSP00000362273 | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | ADP-ribose glycohydrolase ARH3; ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP- ribose and acts on different substrates, such as proteins ADP- ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in [...] | 0.620 |
| ADPRH | ART1 | ENSP00000420200 | ENSP00000250693 | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1; Has ADP-ribosyltransferase activity toward GLP1R. | 0.426 |
| ADPRH | ART5 | ENSP00000420200 | ENSP00000352992 | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | ADP-ribosyltransferase 5. | 0.602 |
| ADPRH | H1-1 | ENSP00000420200 | ENSP00000244573 | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | Histone H1.1; Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). | 0.480 |
| ADPRH | MACROD1 | ENSP00000420200 | ENSP00000255681 | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | ADP-ribose glycohydrolase MACROD1; Removes ADP-ribose from asparatate and glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Plays a role in estrogen signaling. Binds to androgen receptor (AR) and amplifies the transactivation function of AR in response to androgen. May play an important role in carcinogenesis and/or progression of hormone-dependent cancers by feed-forward m [...] | 0.431 |
| ADPRH | SPSB1 | ENSP00000420200 | ENSP00000330221 | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | SPRY domain-containing SOCS box protein 1; Substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Negatively regulates nitric oxide (NO) production and limits cellular toxicity in activated macrophages by mediating the ubiquitination and proteasomal degradation of NOS2. Acts as a bridge which links NOS2 with the ECS E3 ubiquitin ligase complex components ELOC and CUL5. | 0.531 |
| ADPRH | SRPK1 | ENSP00000420200 | ENSP00000362931 | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | SRSF protein kinase 1; Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activiti [...] | 0.463 |
| ADPRH | SRPK2 | ENSP00000420200 | ENSP00000377262 | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | SRSF protein kinase 2 C-terminal; Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates [...] | 0.465 |
| ADPRH | TRIM72 | ENSP00000420200 | ENSP00000312675 | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | Tripartite motif-containing protein 72; Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)- depen [...] | 0.484 |
| ADPRHL2 | ADPRH | ENSP00000362273 | ENSP00000420200 | ADP-ribose glycohydrolase ARH3; ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP- ribose and acts on different substrates, such as proteins ADP- ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in [...] | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | 0.620 |
| ADPRHL2 | MACROD1 | ENSP00000362273 | ENSP00000255681 | ADP-ribose glycohydrolase ARH3; ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP- ribose and acts on different substrates, such as proteins ADP- ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in [...] | ADP-ribose glycohydrolase MACROD1; Removes ADP-ribose from asparatate and glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Plays a role in estrogen signaling. Binds to androgen receptor (AR) and amplifies the transactivation function of AR in response to androgen. May play an important role in carcinogenesis and/or progression of hormone-dependent cancers by feed-forward m [...] | 0.816 |
| ART1 | ADPRH | ENSP00000250693 | ENSP00000420200 | GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1; Has ADP-ribosyltransferase activity toward GLP1R. | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | 0.426 |
| ART1 | ART5 | ENSP00000250693 | ENSP00000352992 | GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1; Has ADP-ribosyltransferase activity toward GLP1R. | ADP-ribosyltransferase 5. | 0.423 |
| ART5 | ADPRH | ENSP00000352992 | ENSP00000420200 | ADP-ribosyltransferase 5. | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | 0.602 |
| ART5 | ART1 | ENSP00000352992 | ENSP00000250693 | ADP-ribosyltransferase 5. | GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1; Has ADP-ribosyltransferase activity toward GLP1R. | 0.423 |
| ART5 | MACROD1 | ENSP00000352992 | ENSP00000255681 | ADP-ribosyltransferase 5. | ADP-ribose glycohydrolase MACROD1; Removes ADP-ribose from asparatate and glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Plays a role in estrogen signaling. Binds to androgen receptor (AR) and amplifies the transactivation function of AR in response to androgen. May play an important role in carcinogenesis and/or progression of hormone-dependent cancers by feed-forward m [...] | 0.566 |
| ART5 | TRIM72 | ENSP00000352992 | ENSP00000312675 | ADP-ribosyltransferase 5. | Tripartite motif-containing protein 72; Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)- depen [...] | 0.478 |
| H1-1 | ADPRH | ENSP00000244573 | ENSP00000420200 | Histone H1.1; Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). | [Protein ADP-ribosylarginine] hydrolase; Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. | 0.480 |