| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| GFM1 | METAP1D | ENSP00000419038 | ENSP00000315152 | Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A- site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mit [...] | 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 (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | 0.682 |
| GFM1 | MTRF1 | ENSP00000419038 | ENSP00000368793 | Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A- site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mit [...] | Peptide chain release factor 1, mitochondrial; Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain non-cognate termination stop codons AGG and AGA | 0.744 |
| GFM1 | PTCD3 | ENSP00000419038 | ENSP00000254630 | Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A- site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mit [...] | Pentatricopeptide repeat domain-containing protein 3, mitochondrial; Mitochondrial RNA-binding protein that has a role in mitochondrial translation | 0.951 |
| GFM1 | RPL35 | ENSP00000419038 | ENSP00000259469 | Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A- site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mit [...] | 60S ribosomal protein L35; Component of the large ribosomal subunit | 0.813 |
| GFM1 | TSFM | ENSP00000419038 | ENSP00000313877 | Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A- site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mit [...] | Elongation factor Ts, mitochondrial; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome; Belongs to the EF-Ts family | 0.940 |
| GFM2 | METAP1D | ENSP00000296805 | ENSP00000315152 | Ribosome-releasing factor 2, mitochondrial; Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily | 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 (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | 0.660 |
| GFM2 | MTRF1 | ENSP00000296805 | ENSP00000368793 | Ribosome-releasing factor 2, mitochondrial; Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily | Peptide chain release factor 1, mitochondrial; Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain non-cognate termination stop codons AGG and AGA | 0.793 |
| GFM2 | PTCD3 | ENSP00000296805 | ENSP00000254630 | Ribosome-releasing factor 2, mitochondrial; Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily | Pentatricopeptide repeat domain-containing protein 3, mitochondrial; Mitochondrial RNA-binding protein that has a role in mitochondrial translation | 0.957 |
| GFM2 | RPL35 | ENSP00000296805 | ENSP00000259469 | Ribosome-releasing factor 2, mitochondrial; Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily | 60S ribosomal protein L35; Component of the large ribosomal subunit | 0.747 |
| GFM2 | TSFM | ENSP00000296805 | ENSP00000313877 | Ribosome-releasing factor 2, mitochondrial; Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily | Elongation factor Ts, mitochondrial; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome; Belongs to the EF-Ts family | 0.622 |
| MAP1B | METAP1D | ENSP00000296755 | ENSP00000315152 | Microtubule-associated protein 1B; Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing; Protein phosphatase 1 regulatory subunits | 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 (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | 0.806 |
| METAP1D | GFM1 | ENSP00000315152 | ENSP00000419038 | 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 (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A- site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mit [...] | 0.682 |
| METAP1D | GFM2 | ENSP00000315152 | ENSP00000296805 | 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 (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | Ribosome-releasing factor 2, mitochondrial; Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily | 0.660 |
| METAP1D | MAP1B | ENSP00000315152 | ENSP00000296755 | 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 (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | Microtubule-associated protein 1B; Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing; Protein phosphatase 1 regulatory subunits | 0.806 |
| METAP1D | METAP2 | ENSP00000315152 | ENSP00000325312 | 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 (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | Methionine aminopeptidase 2; Cotranslationally 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). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N- terminal Met-Val and Met-Thr sequences in vivo; Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic typ [...] | 0.886 |
| METAP1D | MTRF1 | ENSP00000315152 | ENSP00000368793 | 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 (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | Peptide chain release factor 1, mitochondrial; Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain non-cognate termination stop codons AGG and AGA | 0.614 |
| METAP1D | PDF | ENSP00000315152 | ENSP00000288022 | 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 (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | Peptide deformylase, mitochondrial; Removes the formyl group from the N-terminal Met of newly synthesized proteins; Belongs to the polypeptide deformylase family | 0.826 |
| METAP1D | PTCD3 | ENSP00000315152 | ENSP00000254630 | 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 (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | Pentatricopeptide repeat domain-containing protein 3, mitochondrial; Mitochondrial RNA-binding protein that has a role in mitochondrial translation | 0.715 |
| METAP1D | RNPEPL1 | ENSP00000315152 | ENSP00000270357 | 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 (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine; Belongs to the peptidase M1 family | 0.680 |
| METAP1D | RPL35 | ENSP00000315152 | ENSP00000259469 | 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 (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily | 60S ribosomal protein L35; Component of the large ribosomal subunit | 0.627 |
