| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | SUMO1 | ENSP00000339208 | ENSP00000376077 | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Small ubiquitin-related modifier 1; Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for insta [...] | 0.922 |
| 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 |
| DPP8 | UBR2 | ENSP00000339208 | ENSP00000361990 | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | E3 ubiquitin-protein ligase UBR2; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N- terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth. Required for spermatogenesis, promotes, w [...] | 0.634 |
| DPP8 | UBXN4 | ENSP00000339208 | ENSP00000272638 | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | UBX domain-containing protein 4; Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD. | 0.631 |
| DPP8 | WDR90 | ENSP00000339208 | ENSP00000293879 | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | WD repeat-containing protein 90; Required for efficient primary cilium formation. | 0.786 |
| 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 | NLRP1 | ENSP00000262960 | ENSP00000460475 | Dipeptidyl peptidase 9; 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 [...] | 0.956 |