| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | methionyl aminopeptidase type 1D (mitochondrial); Removes the N-terminal methionine from nascent proteins (By similarity). May play a role in colon tumorigenesis | 0.751 |
| METAP1D | MAP1B | ENSP00000315152 | ENSP00000296755 | methionyl aminopeptidase type 1D (mitochondrial); Removes the N-terminal methionine from nascent proteins (By similarity). May play a role in colon tumorigenesis | 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 | 0.751 |
| METAP1D | METAP2 | ENSP00000315152 | ENSP00000325312 | methionyl aminopeptidase type 1D (mitochondrial); Removes the N-terminal methionine from nascent proteins (By similarity). May play a role in colon tumorigenesis | methionyl aminopeptidase 2; Removes the N-terminal methionine from nascent proteins. 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 | 0.923 |
| METAP1D | MRPL3 | ENSP00000315152 | ENSP00000264995 | methionyl aminopeptidase type 1D (mitochondrial); Removes the N-terminal methionine from nascent proteins (By similarity). May play a role in colon tumorigenesis | mitochondrial ribosomal protein L3 | 0.618 |
| METAP1D | MRPL4 | ENSP00000315152 | ENSP00000253099 | methionyl aminopeptidase type 1D (mitochondrial); Removes the N-terminal methionine from nascent proteins (By similarity). May play a role in colon tumorigenesis | mitochondrial ribosomal protein L4 | 0.633 |
| METAP1D | RPL23A | ENSP00000315152 | ENSP00000389103 | methionyl aminopeptidase type 1D (mitochondrial); Removes the N-terminal methionine from nascent proteins (By similarity). May play a role in colon tumorigenesis | ribosomal protein L23a; This protein binds to a specific region on the 26S rRNA (By similarity) | 0.698 |
| METAP1D | RPL35 | ENSP00000315152 | ENSP00000259469 | methionyl aminopeptidase type 1D (mitochondrial); Removes the N-terminal methionine from nascent proteins (By similarity). May play a role in colon tumorigenesis | ribosomal protein L35 | 0.636 |
| METAP1D | RPL4 | ENSP00000315152 | ENSP00000311430 | methionyl aminopeptidase type 1D (mitochondrial); Removes the N-terminal methionine from nascent proteins (By similarity). May play a role in colon tumorigenesis | ribosomal protein L4 | 0.633 |
| METAP1D | RPL5 | ENSP00000315152 | ENSP00000359345 | methionyl aminopeptidase type 1D (mitochondrial); Removes the N-terminal methionine from nascent proteins (By similarity). May play a role in colon tumorigenesis | ribosomal protein L5; Required for rRNA maturation and formation of the 60S ribosomal subunits. This protein binds 5S RNA | 0.661 |
| METAP1D | RPL7 | ENSP00000315152 | ENSP00000339795 | methionyl aminopeptidase type 1D (mitochondrial); Removes the N-terminal methionine from nascent proteins (By similarity). May play a role in colon tumorigenesis | ribosomal protein L7; Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs | 0.633 |
| METAP1D | RPL7L1 | ENSP00000315152 | ENSP00000346063 | methionyl aminopeptidase type 1D (mitochondrial); Removes the N-terminal methionine from nascent proteins (By similarity). May play a role in colon tumorigenesis | ribosomal protein L7-like 1 | 0.633 |
| METAP2 | METAP1D | ENSP00000325312 | ENSP00000315152 | methionyl aminopeptidase 2; Removes the N-terminal methionine from nascent proteins. 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 | methionyl aminopeptidase type 1D (mitochondrial); Removes the N-terminal methionine from nascent proteins (By similarity). May play a role in colon tumorigenesis | 0.923 |
| METAP2 | MRPL3 | ENSP00000325312 | ENSP00000264995 | methionyl aminopeptidase 2; Removes the N-terminal methionine from nascent proteins. 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 | mitochondrial ribosomal protein L3 | 0.611 |
| METAP2 | MRPL4 | ENSP00000325312 | ENSP00000253099 | methionyl aminopeptidase 2; Removes the N-terminal methionine from nascent proteins. 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 | mitochondrial ribosomal protein L4 | 0.633 |
| METAP2 | RPL23A | ENSP00000325312 | ENSP00000389103 | methionyl aminopeptidase 2; Removes the N-terminal methionine from nascent proteins. 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 | ribosomal protein L23a; This protein binds to a specific region on the 26S rRNA (By similarity) | 0.698 |
| METAP2 | RPL35 | ENSP00000325312 | ENSP00000259469 | methionyl aminopeptidase 2; Removes the N-terminal methionine from nascent proteins. 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 | ribosomal protein L35 | 0.636 |
| METAP2 | RPL4 | ENSP00000325312 | ENSP00000311430 | methionyl aminopeptidase 2; Removes the N-terminal methionine from nascent proteins. 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 | ribosomal protein L4 | 0.655 |
| METAP2 | RPL5 | ENSP00000325312 | ENSP00000359345 | methionyl aminopeptidase 2; Removes the N-terminal methionine from nascent proteins. 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 | ribosomal protein L5; Required for rRNA maturation and formation of the 60S ribosomal subunits. This protein binds 5S RNA | 0.661 |
| METAP2 | RPL7 | ENSP00000325312 | ENSP00000339795 | methionyl aminopeptidase 2; Removes the N-terminal methionine from nascent proteins. 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 | ribosomal protein L7; Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs | 0.633 |
| METAP2 | RPL7L1 | ENSP00000325312 | ENSP00000346063 | methionyl aminopeptidase 2; Removes the N-terminal methionine from nascent proteins. 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 | ribosomal protein L7-like 1 | 0.633 |
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