| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CBS | MSRA | ENSP00000381231 | ENSP00000313921 | Cystathionine beta-synthase-like protein; Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L- homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine. Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons. | Mitochondrial peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.401 |
| CBS | MSRB2 | ENSP00000381231 | ENSP00000365693 | Cystathionine beta-synthase-like protein; Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L- homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine. Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons. | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | 0.621 |
| CBS | TXN | ENSP00000381231 | ENSP00000363641 | Cystathionine beta-synthase-like protein; Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L- homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine. Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons. | Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S- nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates [...] | 0.542 |
| LACTB2 | MSRB2 | ENSP00000276590 | ENSP00000365693 | Endoribonuclease LACTB2; Endoribonuclease; cleaves preferentially 3' to purine- pyrimidine dinucleotide motifs in single-stranded RNA. The cleavage product contains a free 3' -OH group. Has no activity with double- stranded RNA or DNA. Required for normal mitochondrial function and cell viability; Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family. | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | 0.606 |
| LACTB2 | PPIL1 | ENSP00000276590 | ENSP00000362803 | Endoribonuclease LACTB2; Endoribonuclease; cleaves preferentially 3' to purine- pyrimidine dinucleotide motifs in single-stranded RNA. The cleavage product contains a free 3' -OH group. Has no activity with double- stranded RNA or DNA. Required for normal mitochondrial function and cell viability; Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family. | Peptidyl-prolyl cis-trans isomerase-like 1; Involved in pre-mRNA splicing as component of the spliceosome. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Belongs to the cyclophilin-type PPIase family. PPIL1 subfamily. | 0.652 |
| MSRA | CBS | ENSP00000313921 | ENSP00000381231 | Mitochondrial peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | Cystathionine beta-synthase-like protein; Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L- homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine. Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons. | 0.401 |
| MSRA | MSRB2 | ENSP00000313921 | ENSP00000365693 | Mitochondrial peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | 0.956 |
| MSRA | TXN | ENSP00000313921 | ENSP00000363641 | Mitochondrial peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S- nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates [...] | 0.936 |
| MSRB2 | CBS | ENSP00000365693 | ENSP00000381231 | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | Cystathionine beta-synthase-like protein; Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L- homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine. Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons. | 0.621 |
| MSRB2 | LACTB2 | ENSP00000365693 | ENSP00000276590 | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | Endoribonuclease LACTB2; Endoribonuclease; cleaves preferentially 3' to purine- pyrimidine dinucleotide motifs in single-stranded RNA. The cleavage product contains a free 3' -OH group. Has no activity with double- stranded RNA or DNA. Required for normal mitochondrial function and cell viability; Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family. | 0.606 |
| MSRB2 | MSRA | ENSP00000365693 | ENSP00000313921 | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | Mitochondrial peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.956 |
| MSRB2 | PPIL1 | ENSP00000365693 | ENSP00000362803 | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | Peptidyl-prolyl cis-trans isomerase-like 1; Involved in pre-mRNA splicing as component of the spliceosome. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Belongs to the cyclophilin-type PPIase family. PPIL1 subfamily. | 0.636 |
| MSRB2 | RAC2 | ENSP00000365693 | ENSP00000249071 | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | Ras-related C3 botulinum toxin substrate 2; Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase. | 0.787 |
| MSRB2 | SDHD | ENSP00000365693 | ENSP00000364699 | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial; Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). | 0.643 |
| MSRB2 | SERPINH1 | ENSP00000365693 | ENSP00000434412 | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | Serpin H1; Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen. | 0.686 |
| MSRB2 | TJAP1 | ENSP00000365693 | ENSP00000361522 | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | Tight junction associated protein 1. | 0.626 |
| MSRB2 | TMBIM6 | ENSP00000365693 | ENSP00000389277 | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | Bax inhibitor 1; Suppressor of apoptosis. Modulates unfolded protein response signaling. Modulates ER calcium homeostasis by acting as a calcium-leak channel. Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation (By similarity). | 0.643 |
| MSRB2 | TXN | ENSP00000365693 | ENSP00000363641 | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S- nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates [...] | 0.761 |
| PPIL1 | LACTB2 | ENSP00000362803 | ENSP00000276590 | Peptidyl-prolyl cis-trans isomerase-like 1; Involved in pre-mRNA splicing as component of the spliceosome. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Belongs to the cyclophilin-type PPIase family. PPIL1 subfamily. | Endoribonuclease LACTB2; Endoribonuclease; cleaves preferentially 3' to purine- pyrimidine dinucleotide motifs in single-stranded RNA. The cleavage product contains a free 3' -OH group. Has no activity with double- stranded RNA or DNA. Required for normal mitochondrial function and cell viability; Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family. | 0.652 |
| PPIL1 | MSRB2 | ENSP00000362803 | ENSP00000365693 | Peptidyl-prolyl cis-trans isomerase-like 1; Involved in pre-mRNA splicing as component of the spliceosome. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Belongs to the cyclophilin-type PPIase family. PPIL1 subfamily. | Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] | 0.636 |
