These are manual checks of primary articles, not a generated research report. Original annotation source fields remain unchanged.
Full article: Harvard author manuscript, DOI 10.1074/jbc.M602648200. The shared human BCL2 reviewer retrieved the PDF; this reviewer independently inspected its methods, results and Figure 3 legend. Whole mouse brain ER supplies the endogenous BCL2–PP2A purification, mouse wild-type/Bcl2-AAA fibroblasts test phosphoregulation, and Bcl2-null fibroblasts expressing human BCL2 supply the ubiquitination assay. Figure 3G immunoprecipitates human BCL2 after strong detergent treatment that dissociates partners, then detects ubiquitin; MG132 increases ubiquitinated BCL2. The assay makes BCL2 the modified substrate, not the ubiquitination machinery. The PP2A assay similarly makes BCL2 the phosphatase substrate. This is distinct from the independently reported calcineurin-substrate targeting role in PMID:12617961.
Exact Figure 3G excerpt: “The BCL-2 IP was probed for ubiquitin.”
The full article supports PP2A binding, phosphoregulation, ER localization and changes in Bcl2-dependent survival. It does not demonstrate Bcl2 executing its own dephosphorylation or polyubiquitination. Source-specific removal of these process annotations does not assert that Bcl2 cannot regulate modification of other proteins in another context.
Full article: McGill et al., Cell 109, 707–718, DOI 10.1016/S0092-8674(02)00762-6, inspected through the PDF web reader. Figure 3 and its Results use anti-MITF chromatin immunoprecipitation in human 501mel melanoma cells; EMSA uses the BCL2 promoter E-box with anti-MITF supershift and wild-type/mutant competitor probes. The demonstrated sequence-specific DNA-binding protein is MITF. BCL2 is the regulated gene, not the DNA-binding protein in these assays. Figure 4 tests MITF-dependent BCL2 expression and promoter activity. This resolves the human donor's GO:0043565 attribution and its transfer to mouse Bcl2; it is not an argument that an antiapoptotic protein could never bind DNA.
Exact Results excerpt: “MITF directly occupies the BCL2 promoter in vivo”.