| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FBXO9 | MEX3C | ENSP00000244426 | ENSP00000385610 | F-box only protein 9; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTO [...] | RNA-binding E3 ubiquitin-protein ligase MEX3C; E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3’ UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation; Ring finger proteins | 0.900 |
| FBXO9 | MIB2 | ENSP00000244426 | ENSP00000426103 | F-box only protein 9; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTO [...] | E3 ubiquitin-protein ligase MIB2; E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors; Ankyrin repeat domain containing | 0.903 |
| FBXO9 | RPS27A | ENSP00000244426 | ENSP00000272317 | F-box only protein 9; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTO [...] | Ubiquitin-40S ribosomal protein S27a; Ubiquitin- Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked- Lys-6-linked may be inv [...] | 0.916 |
| FBXO9 | TRIM32 | ENSP00000244426 | ENSP00000408292 | F-box only protein 9; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTO [...] | E3 ubiquitin-protein ligase TRIM32; Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May ubiquitinate BBS2. May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo; Belongs to the TRIM/RBCC family | 0.902 |
| FBXO9 | TRIM36 | ENSP00000244426 | ENSP00000282369 | F-box only protein 9; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTO [...] | E3 ubiquitin-protein ligase TRIM36; E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Involved in chromosome segregation and cell cycle regulation. May play a role in the acrosome reaction and fertilization; Belongs to the TRIM/RBCC family | 0.902 |
| FBXO9 | TRIM4 | ENSP00000244426 | ENSP00000348216 | F-box only protein 9; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTO [...] | E3 ubiquitin-protein ligase TRIM4; E3 ubiquitin-protein ligase. Mediates ’Lys-63’-linked polyubiquitination of the innate immune receptor DDX58, this linkage doesn’t lead to proteasomal degradation but seems to enhance IFN induction; Belongs to the TRIM/RBCC family | 0.919 |
| FBXO9 | TRIM41 | ENSP00000244426 | ENSP00000320869 | F-box only protein 9; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTO [...] | E3 ubiquitin-protein ligase TRIM41; Functions as an E3 ligase that catalyzes the ubiquitin- mediated degradation of protein kinase C; Ring finger proteins | 0.902 |
| FBXO9 | TRIM69 | ENSP00000244426 | ENSP00000453177 | F-box only protein 9; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTO [...] | E3 ubiquitin-protein ligase TRIM69; May have E3 ubiquitin-protein ligase activity. May play a role in apoptosis; Ring finger proteins | 0.902 |
| FBXO9 | TRIM9 | ENSP00000244426 | ENSP00000298355 | F-box only protein 9; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTO [...] | E3 ubiquitin-protein ligase TRIM9; E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation; Belongs to the TRIM/RBCC family | 0.916 |
| FBXO9 | UBE2N | ENSP00000244426 | ENSP00000316176 | F-box only protein 9; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTO [...] | Ubiquitin-conjugating enzyme E2 N; The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical ’Lys-63’-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the ’Lys-63’-linked poly-ubiquitination of P [...] | 0.904 |
| MEX3C | FBXO9 | ENSP00000385610 | ENSP00000244426 | RNA-binding E3 ubiquitin-protein ligase MEX3C; E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3’ UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation; Ring finger proteins | F-box only protein 9; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTO [...] | 0.900 |
| MEX3C | MIB2 | ENSP00000385610 | ENSP00000426103 | RNA-binding E3 ubiquitin-protein ligase MEX3C; E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3’ UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation; Ring finger proteins | E3 ubiquitin-protein ligase MIB2; E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors; Ankyrin repeat domain containing | 0.906 |
| MEX3C | RPS27A | ENSP00000385610 | ENSP00000272317 | RNA-binding E3 ubiquitin-protein ligase MEX3C; E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3’ UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation; Ring finger proteins | Ubiquitin-40S ribosomal protein S27a; Ubiquitin- Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked- Lys-6-linked may be inv [...] | 0.901 |
| MEX3C | TRIM32 | ENSP00000385610 | ENSP00000408292 | RNA-binding E3 ubiquitin-protein ligase MEX3C; E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3’ UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation; Ring finger proteins | E3 ubiquitin-protein ligase TRIM32; Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May ubiquitinate BBS2. May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo; Belongs to the TRIM/RBCC family | 0.907 |
| MEX3C | TRIM36 | ENSP00000385610 | ENSP00000282369 | RNA-binding E3 ubiquitin-protein ligase MEX3C; E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3’ UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation; Ring finger proteins | E3 ubiquitin-protein ligase TRIM36; E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Involved in chromosome segregation and cell cycle regulation. May play a role in the acrosome reaction and fertilization; Belongs to the TRIM/RBCC family | 0.902 |
| MEX3C | TRIM4 | ENSP00000385610 | ENSP00000348216 | RNA-binding E3 ubiquitin-protein ligase MEX3C; E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3’ UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation; Ring finger proteins | E3 ubiquitin-protein ligase TRIM4; E3 ubiquitin-protein ligase. Mediates ’Lys-63’-linked polyubiquitination of the innate immune receptor DDX58, this linkage doesn’t lead to proteasomal degradation but seems to enhance IFN induction; Belongs to the TRIM/RBCC family | 0.958 |
| MEX3C | TRIM41 | ENSP00000385610 | ENSP00000320869 | RNA-binding E3 ubiquitin-protein ligase MEX3C; E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3’ UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation; Ring finger proteins | E3 ubiquitin-protein ligase TRIM41; Functions as an E3 ligase that catalyzes the ubiquitin- mediated degradation of protein kinase C; Ring finger proteins | 0.902 |
| MEX3C | TRIM69 | ENSP00000385610 | ENSP00000453177 | RNA-binding E3 ubiquitin-protein ligase MEX3C; E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3’ UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation; Ring finger proteins | E3 ubiquitin-protein ligase TRIM69; May have E3 ubiquitin-protein ligase activity. May play a role in apoptosis; Ring finger proteins | 0.903 |
| MEX3C | TRIM9 | ENSP00000385610 | ENSP00000298355 | RNA-binding E3 ubiquitin-protein ligase MEX3C; E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3’ UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation; Ring finger proteins | E3 ubiquitin-protein ligase TRIM9; E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation; Belongs to the TRIM/RBCC family | 0.900 |
| MEX3C | UBE2N | ENSP00000385610 | ENSP00000316176 | RNA-binding E3 ubiquitin-protein ligase MEX3C; E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3’ UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation; Ring finger proteins | Ubiquitin-conjugating enzyme E2 N; The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical ’Lys-63’-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the ’Lys-63’-linked poly-ubiquitination of P [...] | 0.913 |
