node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Dusp11 | Rnf144b | ENSMUSP00000032071 | ENSMUSP00000071017 | RNA/RNP complex-1-interacting phosphatase; Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. In addition, has phosphatase activity with ATP, ADP and O-methylfluorescein phosphate (in vitro). Binds to RNA. May participate in nuclear mRNA metabolism. | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | 0.679 |
Fbxo7 | Rnf144b | ENSMUSP00000120840 | ENSMUSP00000071017 | F-box only protein 7; 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 target proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PRKN to dysfunctional depolarized mitochondria. Promotes MFN1 ubiquitination (By similarity). | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | 0.429 |
Fbxw7 | Rnf144b | ENSMUSP00000103306 | ENSMUSP00000071017 | F-box/WD repeat-containing protein 7; 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 target proteins. Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter bring them to the SCF complex for ubiquitination. Mediates ubiquitination and subsequent degradation of CCNE1 and MYC. Identified substrates include cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1 and pr [...] | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | 0.430 |
Rnf144b | Dusp11 | ENSMUSP00000071017 | ENSMUSP00000032071 | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | RNA/RNP complex-1-interacting phosphatase; Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. In addition, has phosphatase activity with ATP, ADP and O-methylfluorescein phosphate (in vitro). Binds to RNA. May participate in nuclear mRNA metabolism. | 0.679 |
Rnf144b | Fbxo7 | ENSMUSP00000071017 | ENSMUSP00000120840 | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | F-box only protein 7; 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 target proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PRKN to dysfunctional depolarized mitochondria. Promotes MFN1 ubiquitination (By similarity). | 0.429 |
Rnf144b | Fbxw7 | ENSMUSP00000071017 | ENSMUSP00000103306 | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | F-box/WD repeat-containing protein 7; 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 target proteins. Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter bring them to the SCF complex for ubiquitination. Mediates ubiquitination and subsequent degradation of CCNE1 and MYC. Identified substrates include cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1 and pr [...] | 0.430 |
Rnf144b | Rnf183 | ENSMUSP00000071017 | ENSMUSP00000103079 | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | E3 ubiquitin-protein ligase RNF183; Acts as a E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Triggers apoptosis in response to prolonged ER stress by mediating the polyubiquitination and subsequent proteasomal degradation of BCL2L1 (By similarity). May collaborate with FATE1 to restrain BIK protein levels thus regulating apoptotic signaling (By similarity). | 0.479 |
Rnf144b | Rnf223 | ENSMUSP00000071017 | ENSMUSP00000147415 | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | RING finger protein 223. | 0.551 |
Rnf144b | Rnft1 | ENSMUSP00000071017 | ENSMUSP00000020827 | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | E3 ubiquitin-protein ligase RNFT1; E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis. | 0.421 |
Rnf144b | Rnft2 | ENSMUSP00000071017 | ENSMUSP00000112903 | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | RING finger and transmembrane domain-containing protein 2. | 0.435 |
Rnf144b | Tmem150a | ENSMUSP00000071017 | ENSMUSP00000063977 | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | Transmembrane protein 150A; Regulates localization of phosphatidylinositol 4-kinase (PI4K) to the plasma membrane, possibly by reducing the association of TTC7 (TTC7A or TTC7B) with the PI4K complex. Acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis (By similarity). May also play a role in fasting-induced catabolism (By similarity). | 0.415 |
Rnf144b | Traf3 | ENSMUSP00000071017 | ENSMUSP00000021706 | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | TNF receptor-associated factor 3; Regulates pathways leading to the activation of NF-kappa-B and MAP kinases, and plays a central role in the regulation of B-cell survival. Part of signaling pathways leading to the production of cytokines and interferon. Required for normal antibody isotype switching from IgM to IgG. Plays a role T-cell dependent immune responses. Plays a role in the regulation of antiviral responses. Is an essential constituent of several E3 ubiquitin-protein ligase complexes. May have E3 ubiquitin-protein ligase activity and promote 'Lys-63'- linked ubiquitination of [...] | 0.524 |
Rnf144b | Trp73 | ENSMUSP00000071017 | ENSMUSP00000101269 | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | Tumor protein p73; Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein. | 0.437 |
Rnf183 | Rnf144b | ENSMUSP00000103079 | ENSMUSP00000071017 | E3 ubiquitin-protein ligase RNF183; Acts as a E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Triggers apoptosis in response to prolonged ER stress by mediating the polyubiquitination and subsequent proteasomal degradation of BCL2L1 (By similarity). May collaborate with FATE1 to restrain BIK protein levels thus regulating apoptotic signaling (By similarity). | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | 0.479 |
Rnf183 | Rnft1 | ENSMUSP00000103079 | ENSMUSP00000020827 | E3 ubiquitin-protein ligase RNF183; Acts as a E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Triggers apoptosis in response to prolonged ER stress by mediating the polyubiquitination and subsequent proteasomal degradation of BCL2L1 (By similarity). May collaborate with FATE1 to restrain BIK protein levels thus regulating apoptotic signaling (By similarity). | E3 ubiquitin-protein ligase RNFT1; E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis. | 0.491 |
Rnf183 | Rnft2 | ENSMUSP00000103079 | ENSMUSP00000112903 | E3 ubiquitin-protein ligase RNF183; Acts as a E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Triggers apoptosis in response to prolonged ER stress by mediating the polyubiquitination and subsequent proteasomal degradation of BCL2L1 (By similarity). May collaborate with FATE1 to restrain BIK protein levels thus regulating apoptotic signaling (By similarity). | RING finger and transmembrane domain-containing protein 2. | 0.501 |
Rnf223 | Rnf144b | ENSMUSP00000147415 | ENSMUSP00000071017 | RING finger protein 223. | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | 0.551 |
Rnf223 | Rnft1 | ENSMUSP00000147415 | ENSMUSP00000020827 | RING finger protein 223. | E3 ubiquitin-protein ligase RNFT1; E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis. | 0.696 |
Rnf223 | Rnft2 | ENSMUSP00000147415 | ENSMUSP00000112903 | RING finger protein 223. | RING finger and transmembrane domain-containing protein 2. | 0.695 |
Rnft1 | Rnf144b | ENSMUSP00000020827 | ENSMUSP00000071017 | E3 ubiquitin-protein ligase RNFT1; E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis. | E3 ubiquitin-protein ligase RNF144B; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin- dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By s [...] | 0.421 |