| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANKMY1 | RNPEPL1 | ENSP00000385887 | ENSP00000270357 | Ankyrin repeat and MYND domain containing 1 | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | 0.500 |
| ANKMY1 | THAP4 | ENSP00000385887 | ENSP00000385006 | Ankyrin repeat and MYND domain containing 1 | THAP domain containing 4 | 0.709 |
| CAPN10 | RNPEPL1 | ENSP00000375844 | ENSP00000270357 | Calpain-10; Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. May play a role in insulin-stimulated glucose uptake; Belongs to the peptidase C2 family | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | 0.762 |
| CHRND | EIF4E2 | ENSP00000258385 | ENSP00000258416 | Acetylcholine receptor subunit delta; After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane; Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Delta/CHRND sub-subfamily | Eukaryotic translation initiation factor 4E type 2; Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. Acts as a repressor of translation initiation. In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (By similarity) | 0.423 |
| CHRND | RNPEPL1 | ENSP00000258385 | ENSP00000270357 | Acetylcholine receptor subunit delta; After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane; Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Delta/CHRND sub-subfamily | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | 0.523 |
| DKK4 | RNPEPL1 | ENSP00000220812 | ENSP00000270357 | Dickkopf-related protein 4; Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero- posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity) | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | 0.549 |
| EIF4E2 | CHRND | ENSP00000258416 | ENSP00000258385 | Eukaryotic translation initiation factor 4E type 2; Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. Acts as a repressor of translation initiation. In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (By similarity) | Acetylcholine receptor subunit delta; After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane; Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Delta/CHRND sub-subfamily | 0.423 |
| EIF4E2 | RNPEPL1 | ENSP00000258416 | ENSP00000270357 | Eukaryotic translation initiation factor 4E type 2; Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. Acts as a repressor of translation initiation. In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (By similarity) | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | 0.604 |
| METAP1 | METAP2 | ENSP00000296411 | ENSP00000325312 | 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). Required for normal progression through the cell cycle; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | Methionine aminopeptidase 2; 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). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N- terminal Met-Val and Met-Thr sequences in vivo; Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic typ [...] | 0.970 |
| METAP1 | RNPEPL1 | ENSP00000296411 | ENSP00000270357 | 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). Required for normal progression through the cell cycle; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | 0.565 |
| METAP1D | METAP2 | ENSP00000315152 | ENSP00000325312 | Methionine aminopeptidase 1D, mitochondrial; 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | Methionine aminopeptidase 2; 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). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N- terminal Met-Val and Met-Thr sequences in vivo; Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic typ [...] | 0.886 |
| METAP1D | RNPEPL1 | ENSP00000315152 | ENSP00000270357 | Methionine aminopeptidase 1D, mitochondrial; 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | 0.680 |
| METAP2 | METAP1 | ENSP00000325312 | ENSP00000296411 | Methionine aminopeptidase 2; 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). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N- terminal Met-Val and Met-Thr sequences in vivo; Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic typ [...] | 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). Required for normal progression through the cell cycle; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | 0.970 |
| METAP2 | METAP1D | ENSP00000325312 | ENSP00000315152 | Methionine aminopeptidase 2; 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). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N- terminal Met-Val and Met-Thr sequences in vivo; Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic typ [...] | Methionine aminopeptidase 1D, mitochondrial; 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | 0.886 |
| METAP2 | RNPEPL1 | ENSP00000325312 | ENSP00000270357 | Methionine aminopeptidase 2; 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). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N- terminal Met-Val and Met-Thr sequences in vivo; Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic typ [...] | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | 0.565 |
| RNPEPL1 | ANKMY1 | ENSP00000270357 | ENSP00000385887 | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | Ankyrin repeat and MYND domain containing 1 | 0.500 |
| RNPEPL1 | CAPN10 | ENSP00000270357 | ENSP00000375844 | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | Calpain-10; Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. May play a role in insulin-stimulated glucose uptake; Belongs to the peptidase C2 family | 0.762 |
| RNPEPL1 | CHRND | ENSP00000270357 | ENSP00000258385 | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | Acetylcholine receptor subunit delta; After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane; Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Delta/CHRND sub-subfamily | 0.523 |
| RNPEPL1 | DKK4 | ENSP00000270357 | ENSP00000220812 | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | Dickkopf-related protein 4; Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero- posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity) | 0.549 |
| RNPEPL1 | EIF4E2 | ENSP00000270357 | ENSP00000258416 | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | Eukaryotic translation initiation factor 4E type 2; Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. Acts as a repressor of translation initiation. In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (By similarity) | 0.604 |
