node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Blmh | Casp14 | ENSRNOP00000005125 | ENSRNOP00000009643 | 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. | Caspase 14; Belongs to the peptidase C14A family. | 0.812 |
Blmh | Dnajb12 | ENSRNOP00000005125 | ENSRNOP00000049600 | 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. | DnaJ heat shock protein family (Hsp40) member B12. | 0.665 |
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 | LOC102550385 | ENSRNOP00000005125 | ENSRNOP00000065815 | 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. | LYR motif-containing 4; Belongs to the complex I LYR family. | 0.606 |
Blmh | Nudt12 | ENSRNOP00000005125 | ENSRNOP00000061974 | 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. | Nudix (Nucleoside diphosphate linked moiety X)-type motif 12 (Predicted). | 0.711 |
Blmh | Tapbpl | ENSRNOP00000005125 | ENSRNOP00000038874 | 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. | TAP binding protein-like (Predicted). | 0.570 |
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 |
Blmh | Ttc19 | ENSRNOP00000005125 | ENSRNOP00000054591 | 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. | Tetratricopeptide repeat protein 19, mitochondrial; Required for the preservation of the structural and functional integrity of mitochondrial respiratory complex III by allowing the physiological turnover of the Rieske protein UQCRFS1. Involved in the clearance of UQCRFS1 N-terminal fragments, which are produced upon incorporation into the complex III and whose presence is detrimental for its catalytic activity; Belongs to the TTC19 family. | 0.673 |
Blmh | Usp37 | ENSRNOP00000005125 | ENSRNOP00000033308 | 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. | Ubiquitin carboxyl-terminal hydrolase; Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Belongs to the peptidase C19 family. | 0.596 |
Blmh | Wdr73 | ENSRNOP00000005125 | ENSRNOP00000029102 | 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. | Neuromedin B (Predicted), isoform CRA_d. | 0.645 |
Casp14 | Blmh | ENSRNOP00000009643 | ENSRNOP00000005125 | Caspase 14; Belongs to the peptidase C14A 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. | 0.812 |
Dnajb12 | Blmh | ENSRNOP00000049600 | ENSRNOP00000005125 | DnaJ heat shock protein family (Hsp40) member B12. | 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. | 0.665 |
Dnajb12 | LOC102550385 | ENSRNOP00000049600 | ENSRNOP00000065815 | DnaJ heat shock protein family (Hsp40) member B12. | LYR motif-containing 4; Belongs to the complex I LYR family. | 0.634 |
Dnajb12 | Ttc19 | ENSRNOP00000049600 | ENSRNOP00000054591 | DnaJ heat shock protein family (Hsp40) member B12. | Tetratricopeptide repeat protein 19, mitochondrial; Required for the preservation of the structural and functional integrity of mitochondrial respiratory complex III by allowing the physiological turnover of the Rieske protein UQCRFS1. Involved in the clearance of UQCRFS1 N-terminal fragments, which are produced upon incorporation into the complex III and whose presence is detrimental for its catalytic activity; Belongs to the TTC19 family. | 0.732 |
Dnajb12 | Usp37 | ENSRNOP00000049600 | ENSRNOP00000033308 | DnaJ heat shock protein family (Hsp40) member B12. | Ubiquitin carboxyl-terminal hydrolase; Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Belongs to the peptidase C19 family. | 0.617 |
Dnajb12 | Wdr73 | ENSRNOP00000049600 | ENSRNOP00000029102 | DnaJ heat shock protein family (Hsp40) member B12. | Neuromedin B (Predicted), isoform CRA_d. | 0.663 |
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 | 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 |
LOC102550385 | Blmh | ENSRNOP00000065815 | ENSRNOP00000005125 | LYR motif-containing 4; Belongs to the complex I LYR 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. | 0.606 |
LOC102550385 | Dnajb12 | ENSRNOP00000065815 | ENSRNOP00000049600 | LYR motif-containing 4; Belongs to the complex I LYR family. | DnaJ heat shock protein family (Hsp40) member B12. | 0.634 |