| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DCP2 | DOM3Z | ENSP00000373715 | ENSP00000337759 | DCP2 decapping enzyme homolog (S. cerevisiae); Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5’-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking a RNA moiety | dom-3 homolog Z (C. elegans) | 0.680 |
| DCP2 | SKIV2L | ENSP00000373715 | ENSP00000364543 | DCP2 decapping enzyme homolog (S. cerevisiae); Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5’-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking a RNA moiety | superkiller viralicidic activity 2-like (S. cerevisiae) | 0.549 |
| DCP2 | XRN1 | ENSP00000373715 | ENSP00000264951 | DCP2 decapping enzyme homolog (S. cerevisiae); Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5’-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking a RNA moiety | 5’-3’ exoribonuclease 1; Major 5’-3’ exoribonuclease involved in mRNA decay. Required for the 5’-3’-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS) | 0.997 |
| DCP2 | XRN2 | ENSP00000373715 | ENSP00000366396 | DCP2 decapping enzyme homolog (S. cerevisiae); Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5’-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking a RNA moiety | 5’-3’ exoribonuclease 2; Possesses 5’->3’ exoribonuclease activity (By similarity). May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5’ fragment which is subsequently processed to form the mature mRNA and a 3’ fragment which remains attached to the elongating polymerase. The processive degradation of this 3’ fragment by this protein may promote termination of transcription | 0.955 |
| DDX39B | DOM3Z | ENSP00000379475 | ENSP00000337759 | DEAD (Asp-Glu-Ala-Asp) box polypeptide 39B | dom-3 homolog Z (C. elegans) | 0.573 |
| DOM3Z | DCP2 | ENSP00000337759 | ENSP00000373715 | dom-3 homolog Z (C. elegans) | DCP2 decapping enzyme homolog (S. cerevisiae); Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5’-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking a RNA moiety | 0.680 |
| DOM3Z | DDX39B | ENSP00000337759 | ENSP00000379475 | dom-3 homolog Z (C. elegans) | DEAD (Asp-Glu-Ala-Asp) box polypeptide 39B | 0.573 |
| DOM3Z | MTMR11 | ENSP00000337759 | ENSP00000391668 | dom-3 homolog Z (C. elegans) | myotubularin related protein 11 | 0.601 |
| DOM3Z | RDBP | ENSP00000337759 | ENSP00000364578 | dom-3 homolog Z (C. elegans) | RD RNA binding protein; Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex | 0.620 |
| DOM3Z | RPRD1A | ENSP00000337759 | ENSP00000349955 | dom-3 homolog Z (C. elegans) | regulation of nuclear pre-mRNA domain containing 1A; Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. May act as a negative regulator of cyclin-D1 (CCND1) and cyclin-E (CCNE1) in the cell cycle | 0.672 |
| DOM3Z | RPRD1B | ENSP00000337759 | ENSP00000362532 | dom-3 homolog Z (C. elegans) | regulation of nuclear pre-mRNA domain containing 1B; Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3’ end termination site and may allow it to be recruited back to the promoter through prom [...] | 0.681 |
| DOM3Z | SKIV2L | ENSP00000337759 | ENSP00000364543 | dom-3 homolog Z (C. elegans) | superkiller viralicidic activity 2-like (S. cerevisiae) | 0.908 |
| DOM3Z | TJAP1 | ENSP00000337759 | ENSP00000361522 | dom-3 homolog Z (C. elegans) | tight junction associated protein 1 (peripheral) | 0.749 |
| DOM3Z | XRN1 | ENSP00000337759 | ENSP00000264951 | dom-3 homolog Z (C. elegans) | 5’-3’ exoribonuclease 1; Major 5’-3’ exoribonuclease involved in mRNA decay. Required for the 5’-3’-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS) | 0.894 |
| DOM3Z | XRN2 | ENSP00000337759 | ENSP00000366396 | dom-3 homolog Z (C. elegans) | 5’-3’ exoribonuclease 2; Possesses 5’->3’ exoribonuclease activity (By similarity). May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5’ fragment which is subsequently processed to form the mature mRNA and a 3’ fragment which remains attached to the elongating polymerase. The processive degradation of this 3’ fragment by this protein may promote termination of transcription | 0.963 |
| MTMR11 | DOM3Z | ENSP00000391668 | ENSP00000337759 | myotubularin related protein 11 | dom-3 homolog Z (C. elegans) | 0.601 |
| RDBP | DOM3Z | ENSP00000364578 | ENSP00000337759 | RD RNA binding protein; Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex | dom-3 homolog Z (C. elegans) | 0.620 |
| RDBP | SKIV2L | ENSP00000364578 | ENSP00000364543 | RD RNA binding protein; Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex | superkiller viralicidic activity 2-like (S. cerevisiae) | 0.708 |
| RPRD1A | DOM3Z | ENSP00000349955 | ENSP00000337759 | regulation of nuclear pre-mRNA domain containing 1A; Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. May act as a negative regulator of cyclin-D1 (CCND1) and cyclin-E (CCNE1) in the cell cycle | dom-3 homolog Z (C. elegans) | 0.672 |
| RPRD1A | XRN1 | ENSP00000349955 | ENSP00000264951 | regulation of nuclear pre-mRNA domain containing 1A; Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. May act as a negative regulator of cyclin-D1 (CCND1) and cyclin-E (CCNE1) in the cell cycle | 5’-3’ exoribonuclease 1; Major 5’-3’ exoribonuclease involved in mRNA decay. Required for the 5’-3’-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS) | 0.825 |
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