| Annotated protein: | Ubiquitin-protein ligase E3A (EC 2.3.2.26) (HECT-type ubiquitin transferase E3A) (Oncogenic protein-associated protein E6-AP). Gene symbol: UBE3A. Taxonomy: Mus musculus (Mouse). Uniprot ID: O08759 |
| antibody wiki: | |
| SynGO gene info: | SynGO data @ UBE3A |
| Ontology domain: | Cellular Component |
| SynGO term: | synaptic vesicle (GO:0008021) |
| Synapse type(s): | forebrain |
| Annotated paper: | Burette AC, et al. "Subcellular organization of UBE3A in neurons" J Comp Neurol. 2017 Feb 1;525(2):233-251 PMID:27339004 |
| Figure(s): | figure 6, 7 and 8 |
| Annotation description: | Figure 6: Pre-embedding immunogold labeling for UBE3A in the adult mouse forebrain. Labeling for UBE3A is observed in nucleus, endomembranes of the Golgi, presynapse, postsynapse, dendrites, glial membranes, mitochondria. Figure 7: Quantitation of UBE3A immunogold labeling density over different types of profiles in the adult (A) and juvenile (P7, B) mice. The analysis was performed on large EM photomontages of neuropil (each approx. 10x10microM, 15 fields per mouse, three mice per age group). The majority of UBE3A is localized in neuclei and presynapses, localization to postsynapse was approx 4 times less frequent. Figure 8: Pre-embedding immunogold labeling for UBE3A in cerebral cortex at P7. Similar to Figure 6, ubiquitous labeling with some examples of presynaptic localization. Disease relevance in Figure 9: UBE3A staining in the primary visual cortex of adult AS model mice. Figure 9 M,N: Pre-embedding immunogold labeling for UBE3A in cerebral cortex (primary visual cortex, layers I and II). Only very rare silver/gold particles are located over neuronal nuclei (circles in M). In the neuropil, labeling can be seen in presynaptic terminals (inset in N). Conclusion from the authors: UBE3A deficiency is associated with defects in synaptic plasticity, so its synaptic localization is of particular interest. We found UBE3A in the cytoplasm of dendritic spines at levels equivalent to the level found in dendritic shafts. Labeling was rarely directly over postsynaptic densities (PSDs), consistent with findings from biochemical fractionation studies (Gustin et al., 2010) and with the negative findings of several proteomic studies (Cheng et al., 2006; Collins et al., 2006; Bayes et al., 2012) and thus is unlikely to reflect an inaccessibility of PSDs to UBE3A antibodies. Despite a relatively low concentration in PSDs, UBE3A may nevertheless participate locally in postsynaptic regulation, perhaps by regulating the turnover of SAP97 and other synaptic proteins within the cytoplasm of dendritic spines (Matsumoto et al., 2006; Li et al., 2014). ..... Within axon terminals, UBE3A was specifically associated with synaptic vesicles. |
| Evidence tracking, Biological System: | Intact tissue |
| Evidence tracking, Protein Targeting: | Antibody (detection) |
| Evidence tracking, Experiment Assay: | Electron Microscopy |
| Annotator(s): | Noa Lipstein (ORCID:0000-0002-0755-5899) Cordelia Imig (ORCID:0000-0001-7351-8706) Vincent O'connor (ORCID:0000-0003-3185-5709) Nils Brose (ORCID:0000-0003-0938-8534) |
| Lab: | Department of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, 37075 Göttingen, Germany |
| SynGO annotation ID: | 4945 |
| Dataset release (version): | 20231201 |
| View annotation as GO-CAM model: |  |