| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANPEP | NLN | ENSP00000300060 | ENSP00000370372 | alanyl (membrane) aminopeptidase; Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrad [...] | neurolysin (metallopeptidase M3 family); Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A (By similarity) | 0.406 |
| ANPEP | NPEPL1 | ENSP00000300060 | ENSP00000348395 | alanyl (membrane) aminopeptidase; Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrad [...] | aminopeptidase-like 1 | 0.516 |
| ANPEP | THOP1 | ENSP00000300060 | ENSP00000304467 | alanyl (membrane) aminopeptidase; Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrad [...] | thimet oligopeptidase 1; Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. Able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments | 0.505 |
| AQPEP | NPEPL1 | ENSP00000350541 | ENSP00000348395 | Aminopeptidase Q ; Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo- maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met- MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C | aminopeptidase-like 1 | 0.516 |
| ENSG00000174093 | NPEPL1 | ENSP00000308540 | ENSP00000348395 | Uncharacterized protein | aminopeptidase-like 1 | 0.516 |
| ERAP1 | NPEPL1 | ENSP00000296754 | ENSP00000348395 | endoplasmic reticulum aminopeptidase 1; Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play [...] | aminopeptidase-like 1 | 0.516 |
| ERAP2 | NPEPL1 | ENSP00000400376 | ENSP00000348395 | endoplasmic reticulum aminopeptidase 2; Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys | aminopeptidase-like 1 | 0.516 |
| MGC4294 | NPEPL1 | ENSP00000470694 | ENSP00000348395 | HCG1785561; MGC4294 protein | aminopeptidase-like 1 | 0.567 |
| NLN | ANPEP | ENSP00000370372 | ENSP00000300060 | neurolysin (metallopeptidase M3 family); Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A (By similarity) | alanyl (membrane) aminopeptidase; Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrad [...] | 0.406 |
| NLN | NPEPL1 | ENSP00000370372 | ENSP00000348395 | neurolysin (metallopeptidase M3 family); Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A (By similarity) | aminopeptidase-like 1 | 0.563 |
| NLN | NPEPPS | ENSP00000370372 | ENSP00000320324 | neurolysin (metallopeptidase M3 family); Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A (By similarity) | aminopeptidase puromycin sensitive; Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. Digests tau from normal brain more efficiently than tau from Alzheimer disease brain | 0.428 |
| NPEPL1 | ANPEP | ENSP00000348395 | ENSP00000300060 | aminopeptidase-like 1 | alanyl (membrane) aminopeptidase; Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrad [...] | 0.516 |
| NPEPL1 | AQPEP | ENSP00000348395 | ENSP00000350541 | aminopeptidase-like 1 | Aminopeptidase Q ; Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo- maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met- MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C | 0.516 |
| NPEPL1 | ENSG00000174093 | ENSP00000348395 | ENSP00000308540 | aminopeptidase-like 1 | Uncharacterized protein | 0.516 |
| NPEPL1 | ERAP1 | ENSP00000348395 | ENSP00000296754 | aminopeptidase-like 1 | endoplasmic reticulum aminopeptidase 1; Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play [...] | 0.516 |
| NPEPL1 | ERAP2 | ENSP00000348395 | ENSP00000400376 | aminopeptidase-like 1 | endoplasmic reticulum aminopeptidase 2; Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys | 0.516 |
| NPEPL1 | MGC4294 | ENSP00000348395 | ENSP00000470694 | aminopeptidase-like 1 | HCG1785561; MGC4294 protein | 0.567 |
| NPEPL1 | NLN | ENSP00000348395 | ENSP00000370372 | aminopeptidase-like 1 | neurolysin (metallopeptidase M3 family); Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A (By similarity) | 0.563 |
| NPEPL1 | NPEPPS | ENSP00000348395 | ENSP00000320324 | aminopeptidase-like 1 | aminopeptidase puromycin sensitive; Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. Digests tau from normal brain more efficiently than tau from Alzheimer disease brain | 0.516 |
| NPEPL1 | THOP1 | ENSP00000348395 | ENSP00000304467 | aminopeptidase-like 1 | thimet oligopeptidase 1; Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. Able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments | 0.605 |
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