| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CC2D1A | xpnpep3 | ENSDARP00000101762 | ENSDARP00000050244 | Coiled-coil and C2 domain containing 1A. | X-prolyl aminopeptidase (Aminopeptidase P) 3, putative. | 0.740 |
| ak2 | metap1 | ENSDARP00000010686 | ENSDARP00000113818 | Adenylate kinase 2, mitochondrial; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis. | Methionine aminopeptidase 1; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | 0.481 |
| ak2 | xpnpep3 | ENSDARP00000010686 | ENSDARP00000050244 | Adenylate kinase 2, mitochondrial; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis. | X-prolyl aminopeptidase (Aminopeptidase P) 3, putative. | 0.767 |
| akap8l | pbrm1l | ENSDARP00000140942 | ENSDARP00000114800 | A kinase (PRKA) anchor protein 8-like; Belongs to the AKAP95 family. | Polybromo 1,-like. | 0.806 |
| akap8l | xpnpep3 | ENSDARP00000140942 | ENSDARP00000050244 | A kinase (PRKA) anchor protein 8-like; Belongs to the AKAP95 family. | X-prolyl aminopeptidase (Aminopeptidase P) 3, putative. | 0.764 |
| anks3 | xpnpep3 | ENSDARP00000123123 | ENSDARP00000050244 | Ankyrin repeat and sterile alpha motif domain-containing 3. | X-prolyl aminopeptidase (Aminopeptidase P) 3, putative. | 0.773 |
| dsc2l | xpnpep3 | ENSDARP00000090832 | ENSDARP00000050244 | Desmocollin 2-like; Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. | X-prolyl aminopeptidase (Aminopeptidase P) 3, putative. | 0.727 |
| metap1 | ak2 | ENSDARP00000113818 | ENSDARP00000010686 | Methionine aminopeptidase 1; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | Adenylate kinase 2, mitochondrial; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis. | 0.481 |
| metap1 | pitrm1 | ENSDARP00000113818 | ENSDARP00000056293 | Methionine aminopeptidase 1; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | Presequence protease, mitochondrial; Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides; Belongs to the peptidase M16 family. PreP subfamily. | 0.559 |
| metap1 | rnpepl1 | ENSDARP00000113818 | ENSDARP00000002127 | Methionine aminopeptidase 1; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | Arginyl aminopeptidase-like 1. | 0.625 |
| metap1 | xpnpep3 | ENSDARP00000113818 | ENSDARP00000050244 | Methionine aminopeptidase 1; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | X-prolyl aminopeptidase (Aminopeptidase P) 3, putative. | 0.756 |
| osgepl1 | pitrm1 | ENSDARP00000001156 | ENSDARP00000056293 | Probable tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance. | Presequence protease, mitochondrial; Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides; Belongs to the peptidase M16 family. PreP subfamily. | 0.774 |
| osgepl1 | xpnpep3 | ENSDARP00000001156 | ENSDARP00000050244 | Probable tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance. | X-prolyl aminopeptidase (Aminopeptidase P) 3, putative. | 0.819 |
| pbrm1l | akap8l | ENSDARP00000114800 | ENSDARP00000140942 | Polybromo 1,-like. | A kinase (PRKA) anchor protein 8-like; Belongs to the AKAP95 family. | 0.806 |
| pbrm1l | xpnpep3 | ENSDARP00000114800 | ENSDARP00000050244 | Polybromo 1,-like. | X-prolyl aminopeptidase (Aminopeptidase P) 3, putative. | 0.726 |
| pitrm1 | metap1 | ENSDARP00000056293 | ENSDARP00000113818 | Presequence protease, mitochondrial; Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides; Belongs to the peptidase M16 family. PreP subfamily. | Methionine aminopeptidase 1; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | 0.559 |
| pitrm1 | osgepl1 | ENSDARP00000056293 | ENSDARP00000001156 | Presequence protease, mitochondrial; Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides; Belongs to the peptidase M16 family. PreP subfamily. | Probable tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance. | 0.774 |
| pitrm1 | xpnpep3 | ENSDARP00000056293 | ENSDARP00000050244 | Presequence protease, mitochondrial; Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides; Belongs to the peptidase M16 family. PreP subfamily. | X-prolyl aminopeptidase (Aminopeptidase P) 3, putative. | 0.789 |
| rnpepl1 | metap1 | ENSDARP00000002127 | ENSDARP00000113818 | Arginyl aminopeptidase-like 1. | Methionine aminopeptidase 1; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | 0.625 |
| rnpepl1 | xpnpep3 | ENSDARP00000002127 | ENSDARP00000050244 | Arginyl aminopeptidase-like 1. | X-prolyl aminopeptidase (Aminopeptidase P) 3, putative. | 0.745 |