| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABHD12 | DPP9 | ENSP00000365725 | ENSP00000262960 | Lysophosphatidylserine lipase ABHD12; Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes. Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyze [...] | Dipeptidyl peptidase 9; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | 0.610 |
| ATP11A | DPP9 | ENSP00000420387 | ENSP00000262960 | Probable phospholipid-transporting ATPase IH; Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). May be involved in the uptake of farnesyltransferase inhibitor drugs, such as lonafarnib. | Dipeptidyl peptidase 9; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | 0.621 |
| CARD8 | DPP8 | ENSP00000499211 | ENSP00000339208 | Caspase recruitment domain-containing protein 8; Inhibits NF-kappa-B activation. May participate in a regulatory mechanism that coordinates cellular responses controlled by NF-kappa-B transcription factor. May be a component of the inflammasome, a protein complex which also includes PYCARD, NALP2 and CASP1 and whose function would be the activation of proinflammatory caspases. | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | 0.728 |
| CARD8 | DPP9 | ENSP00000499211 | ENSP00000262960 | Caspase recruitment domain-containing protein 8; Inhibits NF-kappa-B activation. May participate in a regulatory mechanism that coordinates cellular responses controlled by NF-kappa-B transcription factor. May be a component of the inflammasome, a protein complex which also includes PYCARD, NALP2 and CASP1 and whose function would be the activation of proinflammatory caspases. | Dipeptidyl peptidase 9; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | 0.963 |
| CARD8 | NLRP1 | ENSP00000499211 | ENSP00000460475 | Caspase recruitment domain-containing protein 8; Inhibits NF-kappa-B activation. May participate in a regulatory mechanism that coordinates cellular responses controlled by NF-kappa-B transcription factor. May be a component of the inflammasome, a protein complex which also includes PYCARD, NALP2 and CASP1 and whose function would be the activation of proinflammatory caspases. | NACHT, LRR and PYD domains-containing protein 1; As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP1, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulat [...] | 0.936 |
| DPP7 | DPP8 | ENSP00000360635 | ENSP00000339208 | Dipeptidyl peptidase 2; Plays an important role in the degradation of some oligopeptides. | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | 0.808 |
| DPP7 | DPP9 | ENSP00000360635 | ENSP00000262960 | Dipeptidyl peptidase 2; Plays an important role in the degradation of some oligopeptides. | Dipeptidyl peptidase 9; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | 0.797 |
| DPP7 | PREP | ENSP00000360635 | ENSP00000499089 | Dipeptidyl peptidase 2; Plays an important role in the degradation of some oligopeptides. | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family. | 0.655 |
| DPP8 | CARD8 | ENSP00000339208 | ENSP00000499211 | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Caspase recruitment domain-containing protein 8; Inhibits NF-kappa-B activation. May participate in a regulatory mechanism that coordinates cellular responses controlled by NF-kappa-B transcription factor. May be a component of the inflammasome, a protein complex which also includes PYCARD, NALP2 and CASP1 and whose function would be the activation of proinflammatory caspases. | 0.728 |
| DPP8 | DPP7 | ENSP00000339208 | ENSP00000360635 | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Dipeptidyl peptidase 2; Plays an important role in the degradation of some oligopeptides. | 0.808 |
| DPP8 | DPP9 | ENSP00000339208 | ENSP00000262960 | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Dipeptidyl peptidase 9; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | 0.900 |
| DPP8 | NLRP1 | ENSP00000339208 | ENSP00000460475 | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | NACHT, LRR and PYD domains-containing protein 1; As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP1, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulat [...] | 0.766 |
| DPP8 | PREP | ENSP00000339208 | ENSP00000499089 | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family. | 0.941 |
| DPP8 | TFDP3 | ENSP00000339208 | ENSP00000385461 | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Transcription factor Dp family member 3; Competitive inhibitor of E2F-mediated transactivation activity. Impairs E2F-mediated cell-cycle progression from G(1) to S phase; Belongs to the E2F/DP family. | 0.841 |
| DPP9 | ABHD12 | ENSP00000262960 | ENSP00000365725 | Dipeptidyl peptidase 9; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Lysophosphatidylserine lipase ABHD12; Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes. Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyze [...] | 0.610 |
| DPP9 | ATP11A | ENSP00000262960 | ENSP00000420387 | Dipeptidyl peptidase 9; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Probable phospholipid-transporting ATPase IH; Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). May be involved in the uptake of farnesyltransferase inhibitor drugs, such as lonafarnib. | 0.621 |
| DPP9 | CARD8 | ENSP00000262960 | ENSP00000499211 | Dipeptidyl peptidase 9; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Caspase recruitment domain-containing protein 8; Inhibits NF-kappa-B activation. May participate in a regulatory mechanism that coordinates cellular responses controlled by NF-kappa-B transcription factor. May be a component of the inflammasome, a protein complex which also includes PYCARD, NALP2 and CASP1 and whose function would be the activation of proinflammatory caspases. | 0.963 |
| DPP9 | DPP7 | ENSP00000262960 | ENSP00000360635 | Dipeptidyl peptidase 9; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Dipeptidyl peptidase 2; Plays an important role in the degradation of some oligopeptides. | 0.797 |
| DPP9 | DPP8 | ENSP00000262960 | ENSP00000339208 | Dipeptidyl peptidase 9; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | 0.900 |
| DPP9 | LZTFL1 | ENSP00000262960 | ENSP00000296135 | Dipeptidyl peptidase 9; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Leucine zipper transcription factor-like protein 1; Regulates ciliary localization of the BBSome complex. Together with the BBSome complex, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. May play a role in neurite outgrowth. May have tumor suppressor function. Belongs to the LZTFL1 family. | 0.681 |