node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
C18orf8 | TMEM241 | ENSP00000269221 | ENSP00000372720 | chromosome 18 open reading frame 8 | transmembrane protein 241 | 0.404 |
CENPW | TMEM241 | ENSP00000357311 | ENSP00000372720 | centromere protein W; Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP [...] | transmembrane protein 241 | 0.507 |
CRELD1 | TMEM241 | ENSP00000321856 | ENSP00000372720 | cysteine-rich with EGF-like domains 1 | transmembrane protein 241 | 0.416 |
CRELD2 | TMEM241 | ENSP00000383938 | ENSP00000372720 | cysteine-rich with EGF-like domains 2 | transmembrane protein 241 | 0.499 |
GFM1 | TMEM241 | ENSP00000419038 | ENSP00000372720 | G elongation factor, mitochondrial 1; 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 m [...] | transmembrane protein 241 | 0.408 |
GFM1 | TXNDC16 | ENSP00000419038 | ENSP00000281741 | G elongation factor, mitochondrial 1; 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 m [...] | thioredoxin domain containing 16 | 0.409 |
GMPPA | TMEM241 | ENSP00000315925 | ENSP00000372720 | GDP-mannose pyrophosphorylase A | transmembrane protein 241 | 0.506 |
SCMH1 | TMEM241 | ENSP00000318094 | ENSP00000372720 | sex comb on midleg homolog 1 (Drosophila); Associates with Polycomb group (PcG) multiprotein complexes; the complex class is required to maintain the transcriptionally repressive state of some genes (By similarity) | transmembrane protein 241 | 0.418 |
TMEM241 | C18orf8 | ENSP00000372720 | ENSP00000269221 | transmembrane protein 241 | chromosome 18 open reading frame 8 | 0.404 |
TMEM241 | CENPW | ENSP00000372720 | ENSP00000357311 | transmembrane protein 241 | centromere protein W; Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP [...] | 0.507 |
TMEM241 | CRELD1 | ENSP00000372720 | ENSP00000321856 | transmembrane protein 241 | cysteine-rich with EGF-like domains 1 | 0.416 |
TMEM241 | CRELD2 | ENSP00000372720 | ENSP00000383938 | transmembrane protein 241 | cysteine-rich with EGF-like domains 2 | 0.499 |
TMEM241 | GFM1 | ENSP00000372720 | ENSP00000419038 | transmembrane protein 241 | G elongation factor, mitochondrial 1; 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 m [...] | 0.408 |
TMEM241 | GMPPA | ENSP00000372720 | ENSP00000315925 | transmembrane protein 241 | GDP-mannose pyrophosphorylase A | 0.506 |
TMEM241 | SCMH1 | ENSP00000372720 | ENSP00000318094 | transmembrane protein 241 | sex comb on midleg homolog 1 (Drosophila); Associates with Polycomb group (PcG) multiprotein complexes; the complex class is required to maintain the transcriptionally repressive state of some genes (By similarity) | 0.418 |
TMEM241 | TXNDC16 | ENSP00000372720 | ENSP00000281741 | transmembrane protein 241 | thioredoxin domain containing 16 | 0.459 |
TXNDC16 | GFM1 | ENSP00000281741 | ENSP00000419038 | thioredoxin domain containing 16 | G elongation factor, mitochondrial 1; 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 m [...] | 0.409 |
TXNDC16 | TMEM241 | ENSP00000281741 | ENSP00000372720 | thioredoxin domain containing 16 | transmembrane protein 241 | 0.459 |