| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FAM86A | KIN | ENSP00000398502 | ENSP00000368881 | Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’ | DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family | 0.631 |
| FAM86A | METTL18 | ENSP00000398502 | ENSP00000307975 | Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’ | Histidine protein methyltransferase 1 homolog; Probable histidine methyltransferase | 0.791 |
| FAM86A | METTL20 | ENSP00000398502 | ENSP00000350353 | Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’ | Electron transfer flavoprotein beta subunit lysine methyltransferase; Protein-lysine methyltransferase that selectively trimethylates the flavoprotein ETFB in mitochondria. Thereby, may negatively regulate the function of ETFB in electron transfer from Acyl-CoA dehydrogenases to the main respiratory chain | 0.792 |
| FAM86A | METTL21A | ENSP00000398502 | ENSP00000415115 | Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’ | Protein N-lysine methyltransferase METTL21A; Protein-lysine methyltransferase that selectively trimethylates residues in heat shock protein 70 (HSP70) family members. Contributes to the in vivo trimethylation of Lys residues in HSPA1 and HSPA8. In vitro methylates ’Lys-561’ in HSPA1, ’Lys- 564’ in HSPA2, ’Lys-585’ in HSPA5, ’Lys-563’ in HSPA6 and ’Lys- 561’ in HSPA8 | 0.818 |
| FAM86A | METTL22 | ENSP00000398502 | ENSP00000371345 | Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’ | Methyltransferase-like protein 22; Protein N-lysine methyltransferase. In vitro methylates KIN; Belongs to the methyltransferase superfamily. METTL22 family | 0.766 |
| FAM86A | METTL23 | ENSP00000398502 | ENSP00000482599 | Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’ | Methyltransferase-like protein 23; Probable methyltransferase | 0.747 |
| FAM86A | N6AMT2 | ENSP00000398502 | ENSP00000372206 | Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’ | EEF1A lysine methyltransferase 1; Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at ’Lys-79’ | 0.681 |
| FAM86A | VCPKMT | ENSP00000398502 | ENSP00000379201 | Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’ | Protein-lysine methyltransferase METTL21D; Protein-lysine N-methyltransferase that specifically trimethylates ’Lys-315’ of VCP/p97; this modification may decrease VCP ATPase activity; Belongs to the methyltransferase superfamily. METTL21 family | 0.804 |
| HRSP12 | METTL22 | ENSP00000254878 | ENSP00000371345 | 2-iminobutanoate/2-iminopropanoate deaminase; Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5’-phosphate-dependent dehydratases including L-threonine dehydratase | Methyltransferase-like protein 22; Protein N-lysine methyltransferase. In vitro methylates KIN; Belongs to the methyltransferase superfamily. METTL22 family | 0.729 |
| KIN | FAM86A | ENSP00000368881 | ENSP00000398502 | DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family | Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’ | 0.631 |
| KIN | METTL18 | ENSP00000368881 | ENSP00000307975 | DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family | Histidine protein methyltransferase 1 homolog; Probable histidine methyltransferase | 0.792 |
| KIN | METTL20 | ENSP00000368881 | ENSP00000350353 | DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family | Electron transfer flavoprotein beta subunit lysine methyltransferase; Protein-lysine methyltransferase that selectively trimethylates the flavoprotein ETFB in mitochondria. Thereby, may negatively regulate the function of ETFB in electron transfer from Acyl-CoA dehydrogenases to the main respiratory chain | 0.672 |
| KIN | METTL21A | ENSP00000368881 | ENSP00000415115 | DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family | Protein N-lysine methyltransferase METTL21A; Protein-lysine methyltransferase that selectively trimethylates residues in heat shock protein 70 (HSP70) family members. Contributes to the in vivo trimethylation of Lys residues in HSPA1 and HSPA8. In vitro methylates ’Lys-561’ in HSPA1, ’Lys- 564’ in HSPA2, ’Lys-585’ in HSPA5, ’Lys-563’ in HSPA6 and ’Lys- 561’ in HSPA8 | 0.740 |
| KIN | METTL22 | ENSP00000368881 | ENSP00000371345 | DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family | Methyltransferase-like protein 22; Protein N-lysine methyltransferase. In vitro methylates KIN; Belongs to the methyltransferase superfamily. METTL22 family | 0.993 |
| KIN | METTL23 | ENSP00000368881 | ENSP00000482599 | DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family | Methyltransferase-like protein 23; Probable methyltransferase | 0.536 |
| KIN | VCPKMT | ENSP00000368881 | ENSP00000379201 | DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family | Protein-lysine methyltransferase METTL21D; Protein-lysine N-methyltransferase that specifically trimethylates ’Lys-315’ of VCP/p97; this modification may decrease VCP ATPase activity; Belongs to the methyltransferase superfamily. METTL21 family | 0.735 |
| METTL18 | FAM86A | ENSP00000307975 | ENSP00000398502 | Histidine protein methyltransferase 1 homolog; Probable histidine methyltransferase | Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on ’Lys-525’ | 0.791 |
| METTL18 | KIN | ENSP00000307975 | ENSP00000368881 | Histidine protein methyltransferase 1 homolog; Probable histidine methyltransferase | DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family | 0.792 |
| METTL18 | METTL20 | ENSP00000307975 | ENSP00000350353 | Histidine protein methyltransferase 1 homolog; Probable histidine methyltransferase | Electron transfer flavoprotein beta subunit lysine methyltransferase; Protein-lysine methyltransferase that selectively trimethylates the flavoprotein ETFB in mitochondria. Thereby, may negatively regulate the function of ETFB in electron transfer from Acyl-CoA dehydrogenases to the main respiratory chain | 0.842 |
| METTL18 | METTL21A | ENSP00000307975 | ENSP00000415115 | Histidine protein methyltransferase 1 homolog; Probable histidine methyltransferase | Protein N-lysine methyltransferase METTL21A; Protein-lysine methyltransferase that selectively trimethylates residues in heat shock protein 70 (HSP70) family members. Contributes to the in vivo trimethylation of Lys residues in HSPA1 and HSPA8. In vitro methylates ’Lys-561’ in HSPA1, ’Lys- 564’ in HSPA2, ’Lys-585’ in HSPA5, ’Lys-563’ in HSPA6 and ’Lys- 561’ in HSPA8 | 0.885 |
