ariadne homolog, ubiquitin-conjugating enzyme E2 binding protein, 1 (Drosophila); E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation

parkinson protein 2, E3 ubiquitin protein ligase (parkin)

ariadne homolog, ubiquitin-conjugating enzyme E2 binding protein, 1 (Drosophila); E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation

ubiquitin-like modifier activating enzyme 1; Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin- E1 thioester and free AMP

ariadne homolog, ubiquitin-conjugating enzyme E2 binding protein, 1 (Drosophila); E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation

ubiquitin C

ariadne homolog, ubiquitin-conjugating enzyme E2 binding protein, 1 (Drosophila); E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation

ubiquitin-conjugating enzyme E2E 2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’- and ’Lys-48’-, as well as ’Lys-63’-linked polyubiquitination

ariadne homolog, ubiquitin-conjugating enzyme E2 binding protein, 1 (Drosophila); E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation

ubiquitin-conjugating enzyme E2L 3; Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine- in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys-11’-linked polyubiquitination. Involved in th [...]

ariadne homolog, ubiquitin-conjugating enzyme E2 binding protein, 1 (Drosophila); E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation

ubiquitin-conjugating enzyme E2L 6; Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3

ariadne homolog, ubiquitin-conjugating enzyme E2 binding protein, 1 (Drosophila); E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation

ubiquitin protein ligase E3A

ariadne homolog 2 (Drosophila); E3 ubiquitin-protein ligase mediating ’Lys-48’-and ’Lys- 63’-linked polyubiquitination and subsequent proteasomal degradation of modified proteins. May play a role in myelopoiesis

ubiquitin C

ariadne homolog 2 (Drosophila); E3 ubiquitin-protein ligase mediating ’Lys-48’-and ’Lys- 63’-linked polyubiquitination and subsequent proteasomal degradation of modified proteins. May play a role in myelopoiesis

ubiquitin-conjugating enzyme E2D 2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’-, as well as ’Lys-48’-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions ’Lys-21’ and/or ’Lys-22’ with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-prime [...]

ariadne homolog 2 (Drosophila); E3 ubiquitin-protein ligase mediating ’Lys-48’-and ’Lys- 63’-linked polyubiquitination and subsequent proteasomal degradation of modified proteins. May play a role in myelopoiesis

ubiquitin-conjugating enzyme E2E 2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’- and ’Lys-48’-, as well as ’Lys-63’-linked polyubiquitination

ariadne homolog 2 (Drosophila); E3 ubiquitin-protein ligase mediating ’Lys-48’-and ’Lys- 63’-linked polyubiquitination and subsequent proteasomal degradation of modified proteins. May play a role in myelopoiesis

ubiquitin-conjugating enzyme E2L 3; Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine- in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys-11’-linked polyubiquitination. Involved in th [...]

ariadne homolog 2 (Drosophila); E3 ubiquitin-protein ligase mediating ’Lys-48’-and ’Lys- 63’-linked polyubiquitination and subsequent proteasomal degradation of modified proteins. May play a role in myelopoiesis

ubiquitin-conjugating enzyme E2L 6; Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3

Cbl proto-oncogene, E3 ubiquitin protein ligase; Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK and other kinases of the [...]

itchy E3 ubiquitin protein ligase

Cbl proto-oncogene, E3 ubiquitin protein ligase; Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK and other kinases of the [...]

neural precursor cell expressed, developmentally down-regulated 4, E3 ubiquitin protein ligase

Cbl proto-oncogene, E3 ubiquitin protein ligase; Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK and other kinases of the [...]

neural precursor cell expressed, developmentally down-regulated 4-like, E3 ubiquitin protein ligase

Cbl proto-oncogene, E3 ubiquitin protein ligase; Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK and other kinases of the [...]

parkinson protein 2, E3 ubiquitin protein ligase (parkin)

Cbl proto-oncogene, E3 ubiquitin protein ligase; Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK and other kinases of the [...]

ubiquitin C

Cbl proto-oncogene, E3 ubiquitin protein ligase; Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK and other kinases of the [...]

ubiquitin-conjugating enzyme E2D 2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’-, as well as ’Lys-48’-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions ’Lys-21’ and/or ’Lys-22’ with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-prime [...]

Cbl proto-oncogene, E3 ubiquitin protein ligase; Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK and other kinases of the [...]

ubiquitin-conjugating enzyme E2L 3; Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine- in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys-11’-linked polyubiquitination. Involved in th [...]

Cbl proto-oncogene, E3 ubiquitin protein ligase; Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK and other kinases of the [...]

ubiquitin protein ligase E3A