Recombinant human UBE3A protein
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Recombinant human UBE3A protein is a Human Full Length protein, in the 2 to 852 aa range, expressed in Baculovirus infected Sf9, with >=81% purity and suitable for Functional studies and SDS-PAGE. The predicted molecular weight of ab198417 protein is 99.8 kDa.
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View Alternative Names
E6AP, EPVE6AP, HPVE6A, UBE3A, Ubiquitin-protein ligase E3A, E6AP ubiquitin-protein ligase, HECT-type ubiquitin transferase E3A, Human papillomavirus E6-associated protein, Oncogenic protein-associated protein E6-AP, Renal carcinoma antigen NY-REN-54
- FuncS
Supplier Data
Functional Studies - Recombinant human UBE3A protein (AB198417)
Activity assay using ab198417.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human UBE3A protein (AB198417)
4-20% SDS-PAGE analysis of 3 μg ab198417 with Coomassie staining.
Reactivity data
Product details
The human UBE3A/E6AP protein ab198417 is useful in conjunction with E1 and E2 for the study of enzyme kinetics, screening inhibitors, and selectivity profiling assays.
Check out our protein gel staining guide for SDS-PAGE here
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The role of UBE3A is connected to protein homeostasis and turnover. It is part of the ubiquitin-proteasome system which regulates the degradation of damaged or unneeded proteins. UBE3A does not work alone; it functions as part of a larger E3 ligase complex. This complex selectively identifies and modifies proteins determining their fate within the cell. The precision of UBE3A in these processes is necessary for normal neural development and synaptic plasticity.
Pathways
UBE3A is involved in the synaptic transmission and neuronal signaling pathways. It interacts with proteins such as HERC2 and RAD18 which are involved in DNA damage response and repair. UBE3A's involvement in these pathways highlights its importance in maintaining neuronal health. This protein's activity influences downstream signaling events affecting processes like synaptic function and neuronal communication.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates (PubMed : 10373495, PubMed : 16772533, PubMed : 19204938, PubMed : 19233847, PubMed : 19325566, PubMed : 19591933, PubMed : 22645313, PubMed : 24273172, PubMed : 24728990, PubMed : 30020076). Several substrates have been identified including the BMAL1, ARC, LAMTOR1, RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B (PubMed : 10373495, PubMed : 19204938, PubMed : 19325566, PubMed : 19591933, PubMed : 22645313, PubMed : 24728990, PubMed : 30020076). Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins (PubMed : 19233847). Finally, UBE3A also promotes its own degradation in vivo. Plays an important role in the regulation of the circadian clock : involved in the ubiquitination of the core clock component BMAL1, leading to its proteasomal degradation (PubMed : 24728990). Acts as transcriptional coactivator of progesterone receptor PGR upon progesterone hormone activation (PubMed : 16772533). Acts as a regulator of synaptic development by mediating ubiquitination and degradation of ARC (By similarity). Required for synaptic remodeling in neurons by mediating ubiquitination and degradation of LAMTOR1, thereby limiting mTORC1 signaling and activity-dependent synaptic remodeling (By similarity). Synergizes with WBP2 in enhancing PGR activity (PubMed : 16772533).. (Microbial infection) Catalyzes the high-risk human papilloma virus E6-mediated ubiquitination of p53/TP53, contributing to the neoplastic progression of cells infected by these viruses.
Post-translational modifications
Phosphorylation at Tyr-659 by ABL1 impairs E3 ligase activity and protects p53/TP53 from degradation in (HPV)-infected cells.
Subcellular localisation
Nucleus
Target data
Product promise
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