| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MAGOH | SUGP1 | ENSP00000360525 | ENSP00000247001 | mago-nashi homolog, proliferation-associated (Drosophila); Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mR [...] | SURP and G patch domain containing 1; Plays a role in pre-mRNA splicing | 0.900 |
| MAGOH | UBC | ENSP00000360525 | ENSP00000344818 | mago-nashi homolog, proliferation-associated (Drosophila); Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mR [...] | ubiquitin C | 0.927 |
| MAGOH | ZC3H11A | ENSP00000360525 | ENSP00000333253 | mago-nashi homolog, proliferation-associated (Drosophila); Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mR [...] | zinc finger CCCH-type containing 11A | 0.997 |
| MRPL53 | PPIB | ENSP00000258105 | ENSP00000300026 | mitochondrial ribosomal protein L53 | peptidylprolyl isomerase B (cyclophilin B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | 0.906 |
| MRPL53 | PPIF | ENSP00000258105 | ENSP00000225174 | mitochondrial ribosomal protein L53 | peptidylprolyl isomerase F; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress- i [...] | 0.909 |
| MRPL53 | RBM27 | ENSP00000258105 | ENSP00000265271 | mitochondrial ribosomal protein L53 | RNA binding motif protein 27 | 0.960 |
| MRPL53 | RBMS1 | ENSP00000258105 | ENSP00000294904 | mitochondrial ribosomal protein L53 | RNA binding motif, single stranded interacting protein 1; Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5’-[AT]CT[AT][AT]T-3’. Probably has a role in DNA replication | 0.961 |
| MRPL53 | SNX3 | ENSP00000258105 | ENSP00000230085 | mitochondrial ribosomal protein L53 | sorting nexin 3 | 0.644 |
| MRPL53 | SUGP1 | ENSP00000258105 | ENSP00000247001 | mitochondrial ribosomal protein L53 | SURP and G patch domain containing 1; Plays a role in pre-mRNA splicing | 0.916 |
| MRPL53 | ZC3H11A | ENSP00000258105 | ENSP00000333253 | mitochondrial ribosomal protein L53 | zinc finger CCCH-type containing 11A | 0.896 |
| PPIB | MRPL53 | ENSP00000300026 | ENSP00000258105 | peptidylprolyl isomerase B (cyclophilin B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | mitochondrial ribosomal protein L53 | 0.906 |
| PPIB | RBMS1 | ENSP00000300026 | ENSP00000294904 | peptidylprolyl isomerase B (cyclophilin B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | RNA binding motif, single stranded interacting protein 1; Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5’-[AT]CT[AT][AT]T-3’. Probably has a role in DNA replication | 0.907 |
| PPIB | SUGP1 | ENSP00000300026 | ENSP00000247001 | peptidylprolyl isomerase B (cyclophilin B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | SURP and G patch domain containing 1; Plays a role in pre-mRNA splicing | 0.911 |
| PPIB | UBC | ENSP00000300026 | ENSP00000344818 | peptidylprolyl isomerase B (cyclophilin B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | ubiquitin C | 0.848 |
| PPIB | ZC3H11A | ENSP00000300026 | ENSP00000333253 | peptidylprolyl isomerase B (cyclophilin B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | zinc finger CCCH-type containing 11A | 0.901 |
| PPIF | MRPL53 | ENSP00000225174 | ENSP00000258105 | peptidylprolyl isomerase F; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress- i [...] | mitochondrial ribosomal protein L53 | 0.909 |
| PPIF | RBMS1 | ENSP00000225174 | ENSP00000294904 | peptidylprolyl isomerase F; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress- i [...] | RNA binding motif, single stranded interacting protein 1; Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5’-[AT]CT[AT][AT]T-3’. Probably has a role in DNA replication | 0.927 |
| PPIF | SUGP1 | ENSP00000225174 | ENSP00000247001 | peptidylprolyl isomerase F; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress- i [...] | SURP and G patch domain containing 1; Plays a role in pre-mRNA splicing | 0.903 |
| PPIF | UBC | ENSP00000225174 | ENSP00000344818 | peptidylprolyl isomerase F; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress- i [...] | ubiquitin C | 0.873 |
| PPIF | ZC3H11A | ENSP00000225174 | ENSP00000333253 | peptidylprolyl isomerase F; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress- i [...] | zinc finger CCCH-type containing 11A | 0.698 |
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