| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AP3S1 | AQPEP | ENSP00000325369 | ENSP00000350541 | adaptor-related protein complex 3, sigma 1 subunit; Part of the AP-3 complex, an adapter-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals | 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 | 0.512 |
| AQPEP | AP3S1 | ENSP00000350541 | ENSP00000325369 | 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 | adaptor-related protein complex 3, sigma 1 subunit; Part of the AP-3 complex, an adapter-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals | 0.512 |
| AQPEP | ARHGAP11B | ENSP00000350541 | ENSP00000392760 | 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 | Rho GTPase activating protein 11B | 0.482 |
| AQPEP | C9orf3 | ENSP00000350541 | ENSP00000364464 | 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 | chromosome 9 open reading frame 3; Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart | 0.632 |
| AQPEP | DNPEP | ENSP00000350541 | ENSP00000273075 | 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 | aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism | 0.539 |
| AQPEP | IFIT3 | ENSP00000350541 | ENSP00000360876 | 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 | interferon-induced protein with tetratricopeptide repeats 3; IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS- mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exihibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1 [...] | 0.577 |
| AQPEP | LAP3 | ENSP00000350541 | ENSP00000226299 | 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 | leucine aminopeptidase 3; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides | 0.546 |
| 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 |
| AQPEP | XPNPEP1 | ENSP00000350541 | ENSP00000421566 | 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 | X-prolyl aminopeptidase (aminopeptidase P) 1, soluble; Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro | 0.584 |
| AQPEP | XPNPEP2 | ENSP00000350541 | ENSP00000360147 | 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 | X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound; A metalloprotease that may play a role in the inflammatory process and other reactions produced in response to injury or infection. May also play a role in the metabolism of the vasodilator bradykinin | 0.584 |
| AQPEP | YARS | ENSP00000350541 | ENSP00000362576 | 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 | tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) (By similarity) | 0.511 |
| ARHGAP11B | AQPEP | ENSP00000392760 | ENSP00000350541 | Rho GTPase activating protein 11B | 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 | 0.482 |
| C9orf3 | AQPEP | ENSP00000364464 | ENSP00000350541 | chromosome 9 open reading frame 3; Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart | 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 | 0.632 |
| C9orf3 | XPNPEP1 | ENSP00000364464 | ENSP00000421566 | chromosome 9 open reading frame 3; Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart | X-prolyl aminopeptidase (aminopeptidase P) 1, soluble; Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro | 0.456 |
| C9orf3 | XPNPEP2 | ENSP00000364464 | ENSP00000360147 | chromosome 9 open reading frame 3; Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart | X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound; A metalloprotease that may play a role in the inflammatory process and other reactions produced in response to injury or infection. May also play a role in the metabolism of the vasodilator bradykinin | 0.422 |
| C9orf3 | YARS | ENSP00000364464 | ENSP00000362576 | chromosome 9 open reading frame 3; Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart | tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) (By similarity) | 0.513 |
| DNPEP | AQPEP | ENSP00000273075 | ENSP00000350541 | aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism | 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 | 0.539 |
| DNPEP | LAP3 | ENSP00000273075 | ENSP00000226299 | aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism | leucine aminopeptidase 3; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides | 0.625 |
| DNPEP | NPEPL1 | ENSP00000273075 | ENSP00000348395 | aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism | aminopeptidase-like 1 | 0.449 |
| DNPEP | XPNPEP1 | ENSP00000273075 | ENSP00000421566 | aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism | X-prolyl aminopeptidase (aminopeptidase P) 1, soluble; Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro | 0.547 |
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