This guide distinguishes the original experiments from database summaries and records the boundaries of the annotation decisions. The historical 50 annotation identities are retained. A current QuickGO snapshot is useful comparison data, but it does not replace those imported rows.
Waterham et al., PMID11519011 tested sequence-verified human full-length DHCR24 in yeast. Methods on expression and enzyme assays and the conversion Results establish NADPH-dependent desmosterol reduction, enhanced by FAD. The assays used yeast homogenates, not purified DHCR24. The 516-residue coding sequence also corrects the much shorter historical KIAA0018 prediction. The core contains one short literal quotation from this source; other annotations cite the same evidence without repeating it.
Current GO:0000246 specifies the EC 1.3.1.71 delta-24(28) reaction involving ergosterol. GO:0050614 specifies EC 1.3.1.72 delta-24 sterol reduction. They are not interchangeable synonyms. Both historical 0000246 source rows are preserved, with proposed replacements to 0050614. The three obsolete pathway-specific rows retain their previously approved replacement to cholesterol biosynthesis.
The official UniProt Q15392 record describes two splice products. Q15392-1 has 516 residues. VSP_056479 replaces its first 76 residues with a 35-residue segment in Q15392-2, producing 475 residues; independent sequence reconstruction matches the downloaded isoform sequence. Historical full-length expression experiments are not evidence that the shorter natural product has the same activity or localization. Reactome's retained 23–516 entity coordinates are a database model, not adopted as proof of physiological signal-peptide cleavage.
PMID11007892 was read as a genuine original, including human H4 construct Methods, microscopy and endogenous organelle-fractionation Results. ER and a lesser Golgi pool were detected; mitochondria were not detected in those conditions. This does not prove exclusive ER residence in every cell or stress state.
The existing PMID22010141 cache remains abstract-only; the missing reference-list entry is restored. Its topology interpretation must be considered alongside PMID27919032, whose original Methods and Results were read and whose cache was fetched normally. In CHO-7 experiments, deletion of the first 56 or 240 residues did not abolish membrane association, and the latter construct remained ER-associated. The C terminus was protease-accessible, while the N terminus remained protected even after partial detergent solubilization. Exact membrane-spanning architecture remains unresolved. Neither an obligatory cleaved signal peptide nor an unequivocal luminal N terminus is asserted.
PMID25637936 uses human DHCR24 and DHCR7 constructs in CHO cells, reciprocal co-immunoprecipitation, hamster-selective depletion and labelled-sterol conversion. DHCR7 is an enzyme, supporting refinement of the existing pair to enzyme binding. Changes in DHCR7 protein abundance, pathway flux and allostery are explicitly left unresolved by the authors. These data do not justify a second duplicate sterol-reductase core or a claim of established direct allosteric activation.
The main PMID15577914 article remains available here only as a primary abstract. Its genuine publisher supplementary Methods and Data were recovered and read. Supplementary Methods describe human p53, MDM2 and DHCR24 constructs, bacterial protein expression, p53 competition and ubiquitination assay designs. Supplementary Data distinguish catalytically inactive N294T/K306N from mutants with impaired p53 association and stress response. Human U2OS experiments also compare MDM2 association of wild-type and L210Q/F211S DHCR24.
This supports a distinct, narrowly described p53-binding core, and specific p53-binding and ubiquitin-protein-ligase-binding replacements for the existing pair annotations. It does not give DHCR24 a ubiquitin-ligase or ROS-consuming activity. One short primary-abstract quotation appears in the core; the supplementary assay evidence is cited without invented quotations. The nuclear annotation is retained as context-dependent: the supplement describes human WI38 fractionation and immunostaining with stress controls, but main-article figure pixels were not inspected. Strong ER attachment in later work makes trafficking a question to resolve, not a sufficient basis to erase a curated stress-specific observation.
PMID30021884 was read in its genuine original. The curated IntAct record EBI-20911008 / IM-26653-2289 identifies human DHCR24–PGRMC1 crosslinking in the Triton-soluble portion of a U2OS nuclear preparation. Both participant sequence identifiers match the canonical proteins. The paper explains that ER can remain with nuclei; the pair therefore does not establish DHCR24 nuclear localization. Crosslinking supports a physical association, not purified binary binding.
OpenCell, PMID35271311 was read from a genuine author manuscript. Its Methods use endogenous tagging in HEK293T cells, digitonin extraction and biological-triplicate affinity proteomics. The author dataset contains a PGRMC1-bait/DHCR24-prey record (CSV line 15878). The prey group includes Q15392, Q15392-2 and A0A0A0MTI1, so the natural isoform is unresolved. Low interaction stoichiometry is not evidence that the detected association is false, and the CSV column labelled pval is not interpreted here as a raw probability.
Official PGRMC1 functions include heme handling and participation in membrane complexes; these do not establish a protein-folding-chaperone or nuclear-receptor partner class for the pair. Both supported generic-binding assertions remain non-core under the explicit project instruction. This instruction is scoped to the ClinGen project. Genericity alone is not contrary evidence.
The genuine PMID16407971 original was read through the mouse and human Results, membrane/plasmin assays, APP-cleavage assays and corresponding Methods. It compares mouse loss of function with full-length human Q15392-HA expression in SH-SY5Y cells. Cholesterol-dependent membrane organization alters protein partitioning, plasminogen recruitment/activation and BACE1 access to APP. The existing plasminogen and APP process assertions are refined to positive regulation of plasminogen activation and negative regulation of APP catabolism, respectively. DHCR24 is not assigned the proteolytic reactions. These are source-specific refinements of existing rows, not new process assertions.
PMID16513830 is abstract-only: mouse cholesterol-depleted fibroblasts show altered insulin-receptor/caveolin partitioning. PMID17210742 is also abstract-only and reports rat ACTH responsiveness. Its expression/distribution evidence does not settle the human process transfer, which is undecided. PMID14684813 is title-only, so the tissue- and male-genitalia-development transfers remain undecided. The clinical PMID12457401 abstract supports developmental disease and biochemical deficiency but does not settle process allocation; that row is undecided too.
The skin/barrier phenotype is explicit in the PMID16410790 abstract. The existing mouse-to-human skin assertions remain undecided because their original developmental allocation and controls could not be read. For the membrane-proteomics row from PMID19946888, the target peptide assignment and exact fraction remain unavailable. Independent localization experiments nevertheless establish membrane association, so the broad row proposes the supported ER-membrane term. This is a gene-level refinement using independent evidence; the YTS HDA fraction itself is not claimed to resolve ER. PMID16321981 provides abstract-level mouse sterol context, while direct human chemistry independently establishes cholesterol-synthesis participation. Failed original-recovery attempts are recorded as access limits, not negative biological results.
The current PTHR10801 tree places human DHCR24 under the historical nodes. Reused, timestamped PAINT IBD/leaf files show a membrane assertion replacing historical cytoplasm and a changed placement for 0000246. Mouse, rat, human and plant donor identities and their actual descendant paths were reconstructed. The target among descendant evidence is legitimate grounding, not circularity. The chemistry-specific replacement is based on the term definition and human assay, not donor count.
ARBA00027309 has an exact matching FunFam 3.30.465.10:FF:000032 alternative branch on the official target record. InterPro matches IPR006094, IPR036318 and IPR016166 supply the actual flavin-binding mappings; their coordinates and target matches were checked. Family-level examples of covalent flavin attachment are not transferred to DHCR24.
The three previously missing reaction caches were fetched through the normal Reactome fetcher. Each reaction resolves through CatalystActivity 196404, human Q15392 entity 196414 and ER-membrane compartment 0005789. Source names alone were not used for attribution. Existing publications, provider research, pathway files and history are unchanged.
The topology and APP/plasminogen rows now contain short literal excerpts from their cached originals. The two core excerpts remain single-use anchors. References elsewhere point to the same evidence without repeating quotations.
For Greeve et al., original Results on intracellular localization, the endogenous human H4 fractionation result is: “Seladin-1 was clearly present in the Golgi and ER fractions”. The membrane row separately uses a five-word cached Discussion excerpt. Although its cache is marked full_text_available: true, the quoted fractionation Results passage is absent from that extraction; it was read in the genuine original article. Tagged imaging and endogenous fractionation are distinct observations, and neither establishes exclusive ER residence.
For Luu et al., original Results on reciprocal immunoprecipitation, the authors state “we used a more stringent RIPA buffer” and “DHCR7 immunoprecipitation also pulled down DHCR24”. The binding row uses a short cached abstract excerpt. This cache also has a true full-text flag but omits these Results passages; the exact RIPA and reverse-pull-down details come from the recovered original. Human constructs were expressed in CHO cells. Cellular regulation is demonstrated, while altered DHCR7 abundance, sterol flux and direct allostery remain alternatives in the Discussion.
The separate p53-binding core is a molecular interaction mechanism supported by human recombinant assays and separation-of-function data in the genuine publisher supplement. The broader proliferation/Ras phenotypes and reported nuclear pool remain contextual observations. No nuclear or ER location is assigned to the binding core: its knowledge gap explicitly records that endogenous interaction localization and trafficking are unresolved. The main article remains abstract-only here; no unseen main-article figures are claimed.