Specification
| Organism | Homo sapiens (Human) |
| Expression Host | E.coli |
| Tag Info | N-terminal 6xHis-SUMO-tagged |
| Purity | Greater than 85% by SDS-PAGE |
| Uniprot ID | P61077 |
| Gene Names | UBE2D3 |
| Alternative Names | Ubiquitin carrier protein D3Ubiquitin-conjugating enzyme E2(17)KB 3Ubiquitin-conjugating enzyme E2-17KDA 3Ubiquitin-protein ligase D3 |
| Expression Region | Full Length(1-147aa ) |
| Molecular Weight | 32.7 kDa |
| Protein Sequence | MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM |
| Form | Liquid or Lyophilization |
| Buffer | The default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol if the delivery form is liquid. The lyophilization buffer is Tris/PBS-based buffer, 6% Trehalose, pH 8.0 if the delivery form is lyophilized powder. Please contact us if you have any special requirment. |
| Reconstitution | Please reconstitute protein in deionized sterile water and we recommend that briefly centrifuge thevial prior to opening the vial .We recommend aliquot for long-term storage at -20℃/-80℃. |
Background
| Relevance | 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-primed NFKBIA-linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukia protein nuclear body (PML-NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma mbrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction . |
| Involvement in Disease | |
| Subcellular Location | Cell membrane, Peripheral membrane protein, Endosome membrane, Peripheral membrane protein |
| Protein Families | Ubiquitin-conjugating enzyme family |
| Tissue Specificity | UBE2D3 |
QC Data
| Note | Please contact us for QC Data |
| Product Image (Reference Only) |  |