node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Atg5 | Tpp2 | ENSRNOP00000075339 | ENSRNOP00000074045 | Autophagy protein 5; Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3- like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is ess [...] | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | 0.529 |
Blmh | Erap1 | ENSRNOP00000005125 | ENSRNOP00000013625 | Bleomycin hydrolase; The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B- aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity (By similarity). Binds single-stranded DNA with higher affinity than double-stranded DNA. May play an important role in the metabolism of antibiotics; Belongs to the peptidase C1 family. | 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 [...] | 0.615 |
Blmh | Tpp2 | ENSRNOP00000005125 | ENSRNOP00000074045 | Bleomycin hydrolase; The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B- aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity (By similarity). Binds single-stranded DNA with higher affinity than double-stranded DNA. May play an important role in the metabolism of antibiotics; Belongs to the peptidase C1 family. | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | 0.608 |
Ctsa | Tpp2 | ENSRNOP00000062425 | ENSRNOP00000074045 | Carboxypeptidase; Belongs to the peptidase S10 family. | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | 0.539 |
Erap1 | Blmh | ENSRNOP00000013625 | ENSRNOP00000005125 | 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 [...] | Bleomycin hydrolase; The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B- aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity (By similarity). Binds single-stranded DNA with higher affinity than double-stranded DNA. May play an important role in the metabolism of antibiotics; Belongs to the peptidase C1 family. | 0.615 |
Erap1 | Tapbp | ENSRNOP00000013625 | ENSRNOP00000045630 | 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 [...] | Tap-binding protein (Tapasin). | 0.810 |
Erap1 | Tpp2 | ENSRNOP00000013625 | ENSRNOP00000074045 | 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 [...] | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | 0.626 |
Fkbp4 | Tpp2 | ENSRNOP00000008737 | ENSRNOP00000074045 | Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90) (By similarity). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. May have a protective role against oxidative stress in mitochondria (By similarity). Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promo [...] | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | 0.592 |
Mipep | Tpp2 | ENSRNOP00000073167 | ENSRNOP00000074045 | Mitochondrial intermediate peptidase; Cleaves proteins, imported into the mitochondrion, to their mature size; Belongs to the peptidase M3 family. | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | 0.482 |
Nrdc | Thop1 | ENSRNOP00000010462 | ENSRNOP00000027045 | Nardilysin; Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs. | Thimet oligopeptidase; Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. | 0.554 |
Nrdc | Tpp2 | ENSRNOP00000010462 | ENSRNOP00000074045 | Nardilysin; Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs. | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | 0.483 |
Qser1 | Tpp2 | ENSRNOP00000053652 | ENSRNOP00000074045 | Glutamine and serine rich 1 (Predicted). | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | 0.636 |
Tapbp | Erap1 | ENSRNOP00000045630 | ENSRNOP00000013625 | Tap-binding protein (Tapasin). | 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 [...] | 0.810 |
Tapbp | Tpp2 | ENSRNOP00000045630 | ENSRNOP00000074045 | Tap-binding protein (Tapasin). | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | 0.481 |
Thop1 | Nrdc | ENSRNOP00000027045 | ENSRNOP00000010462 | Thimet oligopeptidase; Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. | Nardilysin; Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs. | 0.554 |
Thop1 | Tpp2 | ENSRNOP00000027045 | ENSRNOP00000074045 | Thimet oligopeptidase; Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | 0.551 |
Tpp2 | Atg5 | ENSRNOP00000074045 | ENSRNOP00000075339 | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | Autophagy protein 5; Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3- like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is ess [...] | 0.529 |
Tpp2 | Blmh | ENSRNOP00000074045 | ENSRNOP00000005125 | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | Bleomycin hydrolase; The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B- aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity (By similarity). Binds single-stranded DNA with higher affinity than double-stranded DNA. May play an important role in the metabolism of antibiotics; Belongs to the peptidase C1 family. | 0.608 |
Tpp2 | Ctsa | ENSRNOP00000074045 | ENSRNOP00000062425 | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | Carboxypeptidase; Belongs to the peptidase S10 family. | 0.539 |
Tpp2 | Erap1 | ENSRNOP00000074045 | ENSRNOP00000013625 | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity); Belongs to the peptidase S8 family. | 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 [...] | 0.626 |