node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Atp23 | Immp2l | ENSMUSP00000128382 | ENSMUSP00000118779 | Mitochondrial inner membrane protease ATP23 homolog. | Mitochondrial inner membrane protease subunit 2; Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO (By similarity). | 0.593 |
Atp23 | Mipep | ENSMUSP00000128382 | ENSMUSP00000069840 | Mitochondrial inner membrane protease ATP23 homolog. | Mitochondrial intermediate peptidase; Cleaves proteins, imported into the mitochondrion, to their mature size; Belongs to the peptidase M3 family. | 0.690 |
Atp23 | Oma1 | ENSMUSP00000128382 | ENSMUSP00000045269 | Mitochondrial inner membrane protease ATP23 homolog. | Metalloendopeptidase OMA1, mitochondrial; Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion. May also cleave UQCC3 under these conditions. Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions. Belongs to the peptidase [...] | 0.746 |
Atp23 | Pmpca | ENSMUSP00000128382 | ENSMUSP00000075762 | Mitochondrial inner membrane protease ATP23 homolog. | Mitochondrial-processing peptidase subunit alpha; Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins. | 0.517 |
Atp23 | Xpnpep3 | ENSMUSP00000128382 | ENSMUSP00000132822 | Mitochondrial inner membrane protease ATP23 homolog. | Xaa-Pro aminopeptidase 3; Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Leu-Pro-Ala. Also shows low activity towards peptides with Ala or Ser at the P1 position. Promotes TNFRSF1B- mediated phosphorylation of MAPK8/JNK1 and MAPK9/JNK2, suggesting a function as an adapter protein for TNFRSF1B; the effect is independent of XPNPEP3 peptidase activity. May inhibit apoptotic cell death induced via TNF-TNFRSF1B signaling. | 0.543 |
Dnpep | Lap3 | ENSMUSP00000140864 | ENSMUSP00000040222 | 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 (By similarity). | Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity). | 0.619 |
Dnpep | Xpnpep3 | ENSMUSP00000140864 | ENSMUSP00000132822 | 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 (By similarity). | Xaa-Pro aminopeptidase 3; Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Leu-Pro-Ala. Also shows low activity towards peptides with Ala or Ser at the P1 position. Promotes TNFRSF1B- mediated phosphorylation of MAPK8/JNK1 and MAPK9/JNK2, suggesting a function as an adapter protein for TNFRSF1B; the effect is independent of XPNPEP3 peptidase activity. May inhibit apoptotic cell death induced via TNF-TNFRSF1B signaling. | 0.584 |
Immp2l | Atp23 | ENSMUSP00000118779 | ENSMUSP00000128382 | Mitochondrial inner membrane protease subunit 2; Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO (By similarity). | Mitochondrial inner membrane protease ATP23 homolog. | 0.593 |
Immp2l | Metap1d | ENSMUSP00000118779 | ENSMUSP00000048190 | Mitochondrial inner membrane protease subunit 2; Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO (By similarity). | Methionine aminopeptidase 1D, mitochondrial; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | 0.426 |
Immp2l | Mipep | ENSMUSP00000118779 | ENSMUSP00000069840 | Mitochondrial inner membrane protease subunit 2; Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO (By similarity). | Mitochondrial intermediate peptidase; Cleaves proteins, imported into the mitochondrion, to their mature size; Belongs to the peptidase M3 family. | 0.730 |
Immp2l | Oma1 | ENSMUSP00000118779 | ENSMUSP00000045269 | Mitochondrial inner membrane protease subunit 2; Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO (By similarity). | Metalloendopeptidase OMA1, mitochondrial; Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion. May also cleave UQCC3 under these conditions. Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions. Belongs to the peptidase [...] | 0.496 |
Immp2l | Pmpca | ENSMUSP00000118779 | ENSMUSP00000075762 | Mitochondrial inner membrane protease subunit 2; Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO (By similarity). | Mitochondrial-processing peptidase subunit alpha; Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins. | 0.647 |
Immp2l | Pmpcb | ENSMUSP00000118779 | ENSMUSP00000030882 | Mitochondrial inner membrane protease subunit 2; Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO (By similarity). | Mitochondrial-processing peptidase subunit beta; Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (By similarity). Preferentially, cleaves after an arginine at position P2 (By similarity). Required for PINK1 turnover by coupling PINK1 mitochondrial import and cleavage, which results in subsequent PINK1 proteolysis (By similarity). Belongs to the peptidase M16 family. | 0.556 |
Immp2l | Xpnpep3 | ENSMUSP00000118779 | ENSMUSP00000132822 | Mitochondrial inner membrane protease subunit 2; Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO (By similarity). | Xaa-Pro aminopeptidase 3; Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Leu-Pro-Ala. Also shows low activity towards peptides with Ala or Ser at the P1 position. Promotes TNFRSF1B- mediated phosphorylation of MAPK8/JNK1 and MAPK9/JNK2, suggesting a function as an adapter protein for TNFRSF1B; the effect is independent of XPNPEP3 peptidase activity. May inhibit apoptotic cell death induced via TNF-TNFRSF1B signaling. | 0.625 |
Lap3 | Dnpep | ENSMUSP00000040222 | ENSMUSP00000140864 | Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity). | 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 (By similarity). | 0.619 |
Lap3 | Xpnpep3 | ENSMUSP00000040222 | ENSMUSP00000132822 | Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity). | Xaa-Pro aminopeptidase 3; Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Leu-Pro-Ala. Also shows low activity towards peptides with Ala or Ser at the P1 position. Promotes TNFRSF1B- mediated phosphorylation of MAPK8/JNK1 and MAPK9/JNK2, suggesting a function as an adapter protein for TNFRSF1B; the effect is independent of XPNPEP3 peptidase activity. May inhibit apoptotic cell death induced via TNF-TNFRSF1B signaling. | 0.648 |
Metap1d | Immp2l | ENSMUSP00000048190 | ENSMUSP00000118779 | Methionine aminopeptidase 1D, mitochondrial; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | Mitochondrial inner membrane protease subunit 2; Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO (By similarity). | 0.426 |
Metap1d | Mipep | ENSMUSP00000048190 | ENSMUSP00000069840 | Methionine aminopeptidase 1D, mitochondrial; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | Mitochondrial intermediate peptidase; Cleaves proteins, imported into the mitochondrion, to their mature size; Belongs to the peptidase M3 family. | 0.427 |
Metap1d | Pmpca | ENSMUSP00000048190 | ENSMUSP00000075762 | Methionine aminopeptidase 1D, mitochondrial; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | Mitochondrial-processing peptidase subunit alpha; Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins. | 0.514 |
Metap1d | Pmpcb | ENSMUSP00000048190 | ENSMUSP00000030882 | Methionine aminopeptidase 1D, mitochondrial; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. | Mitochondrial-processing peptidase subunit beta; Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (By similarity). Preferentially, cleaves after an arginine at position P2 (By similarity). Required for PINK1 turnover by coupling PINK1 mitochondrial import and cleavage, which results in subsequent PINK1 proteolysis (By similarity). Belongs to the peptidase M16 family. | 0.482 |