node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Mid1 | Mid2 | ENSMUSP00000107733 | ENSMUSP00000108617 | E3 ubiquitin-protein ligase Midline-1; Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. | Probable E3 ubiquitin-protein ligase MID2; May play a role in microtubule stabilization. Belongs to the TRIM/RBCC family. | 0.459 |
Mid1 | Pml | ENSMUSP00000107733 | ENSMUSP00000082816 | E3 ubiquitin-protein ligase Midline-1; Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. | Protein PML; Functions via its association with PML-nuclear bodies (PML- NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosph [...] | 0.537 |
Mid1 | Tmlhe | ENSMUSP00000107733 | ENSMUSP00000111624 | E3 ubiquitin-protein ligase Midline-1; Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. | Trimethyllysine dioxygenase, mitochondrial; Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML); Belongs to the gamma-BBH/TMLD family. | 0.493 |
Mid1 | Trat1 | ENSMUSP00000107733 | ENSMUSP00000155986 | E3 ubiquitin-protein ligase Midline-1; Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. | T-cell receptor-associated transmembrane adapter 1; Stabilizes the TCR (T-cell antigen receptor)/CD3 complex at the surface of T-cells. | 0.654 |
Mid1 | Trim15 | ENSMUSP00000107733 | ENSMUSP00000133953 | E3 ubiquitin-protein ligase Midline-1; Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. | Tripartite motif-containing 15. | 0.409 |
Mid2 | Mid1 | ENSMUSP00000108617 | ENSMUSP00000107733 | Probable E3 ubiquitin-protein ligase MID2; May play a role in microtubule stabilization. Belongs to the TRIM/RBCC family. | E3 ubiquitin-protein ligase Midline-1; Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. | 0.459 |
Mid2 | Pml | ENSMUSP00000108617 | ENSMUSP00000082816 | Probable E3 ubiquitin-protein ligase MID2; May play a role in microtubule stabilization. Belongs to the TRIM/RBCC family. | Protein PML; Functions via its association with PML-nuclear bodies (PML- NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosph [...] | 0.643 |
Mid2 | Tmlhe | ENSMUSP00000108617 | ENSMUSP00000111624 | Probable E3 ubiquitin-protein ligase MID2; May play a role in microtubule stabilization. Belongs to the TRIM/RBCC family. | Trimethyllysine dioxygenase, mitochondrial; Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML); Belongs to the gamma-BBH/TMLD family. | 0.492 |
Mid2 | Trat1 | ENSMUSP00000108617 | ENSMUSP00000155986 | Probable E3 ubiquitin-protein ligase MID2; May play a role in microtubule stabilization. Belongs to the TRIM/RBCC family. | T-cell receptor-associated transmembrane adapter 1; Stabilizes the TCR (T-cell antigen receptor)/CD3 complex at the surface of T-cells. | 0.668 |
Mid2 | Trim15 | ENSMUSP00000108617 | ENSMUSP00000133953 | Probable E3 ubiquitin-protein ligase MID2; May play a role in microtubule stabilization. Belongs to the TRIM/RBCC family. | Tripartite motif-containing 15. | 0.425 |
Mid2 | Trim21 | ENSMUSP00000108617 | ENSMUSP00000033264 | Probable E3 ubiquitin-protein ligase MID2; May play a role in microtubule stabilization. Belongs to the TRIM/RBCC family. | E3 ubiquitin-protein ligase TRIM21; E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degrad [...] | 0.518 |
Mid2 | Trim34a | ENSMUSP00000108617 | ENSMUSP00000055058 | Probable E3 ubiquitin-protein ligase MID2; May play a role in microtubule stabilization. Belongs to the TRIM/RBCC family. | Tripartite motif-containing protein 34A; May function as antiviral protein and may contribute to the defense against retroviral infections; Belongs to the TRIM/RBCC family. | 0.541 |
Mid2 | Trim6 | ENSMUSP00000108617 | ENSMUSP00000095782 | Probable E3 ubiquitin-protein ligase MID2; May play a role in microtubule stabilization. Belongs to the TRIM/RBCC family. | Tripartite motif-containing protein 6; E3 ubiquitin-protein ligase which ubiquitinates MYC and inhibits its transcription activation activity, maintaining the pluripotency of embryonic stem cells. Involved in the synthesis of unanchored K48-linked polyubiquitin chains which interact with and activate the serine/threonine kinase IKBKE, leading to phosphorylation of STAT1 and stimulation of an antiviral response ; Belongs to the TRIM/RBCC family. | 0.476 |
Pml | Mid1 | ENSMUSP00000082816 | ENSMUSP00000107733 | Protein PML; Functions via its association with PML-nuclear bodies (PML- NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosph [...] | E3 ubiquitin-protein ligase Midline-1; Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. | 0.537 |
Pml | Mid2 | ENSMUSP00000082816 | ENSMUSP00000108617 | Protein PML; Functions via its association with PML-nuclear bodies (PML- NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosph [...] | Probable E3 ubiquitin-protein ligase MID2; May play a role in microtubule stabilization. Belongs to the TRIM/RBCC family. | 0.643 |
Pml | Tmlhe | ENSMUSP00000082816 | ENSMUSP00000111624 | Protein PML; Functions via its association with PML-nuclear bodies (PML- NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosph [...] | Trimethyllysine dioxygenase, mitochondrial; Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML); Belongs to the gamma-BBH/TMLD family. | 0.521 |
Pml | Trat1 | ENSMUSP00000082816 | ENSMUSP00000155986 | Protein PML; Functions via its association with PML-nuclear bodies (PML- NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosph [...] | T-cell receptor-associated transmembrane adapter 1; Stabilizes the TCR (T-cell antigen receptor)/CD3 complex at the surface of T-cells. | 0.742 |
Pml | Trim15 | ENSMUSP00000082816 | ENSMUSP00000133953 | Protein PML; Functions via its association with PML-nuclear bodies (PML- NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosph [...] | Tripartite motif-containing 15. | 0.489 |
Pml | Trim21 | ENSMUSP00000082816 | ENSMUSP00000033264 | Protein PML; Functions via its association with PML-nuclear bodies (PML- NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosph [...] | E3 ubiquitin-protein ligase TRIM21; E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degrad [...] | 0.618 |
Pml | Trim34a | ENSMUSP00000082816 | ENSMUSP00000055058 | Protein PML; Functions via its association with PML-nuclear bodies (PML- NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosph [...] | Tripartite motif-containing protein 34A; May function as antiviral protein and may contribute to the defense against retroviral infections; Belongs to the TRIM/RBCC family. | 0.478 |