The 54 genuine source assertions are retained with their original term, evidence, reference, qualifier and supporting entities. All have individual assessments: 40 ACCEPT, nine MODIFY, four KEEP_AS_NON_CORE and one UNDECIDED. No NEW annotation is proposed. The compact source evidence index identifies public datasets, exact target records, assay limits and preserved repository sources; it does not substitute for the underlying primary evidence.
The normal Falcon attempt ended after Edison authentication HTTP 503 and exhausted configured retries. The configured Perplexity fallback ended with HTTP 401 insufficient quota. Neither produced a provider report. This is manual synthesis, using genuine publication retrieval and independently read primary material; no manually authored text is labeled as provider output. Failed access bodies and earlier source variants remain in the audit packet. Protected repository caches and GO-CAM sources are unchanged, including abstract-only flags where an original was recovered separately.
CTPS1 catalyzes ATP-dependent amination of UTP, using glutamine as the nitrogen source. Human protein expressed in yeast has been purified and tested directly; human patient deficiency, knockdown and reconstitution provide complementary cellular evidence (PMID:17189248, PMID:17463002, PMID:28459447, PMID:24870241). The 2005 complete abstract supports human complementation of the yeast ura7/ura8 double mutant, but its full original remains unavailable. Its glucose-associated phosphorylation observation does not establish direct PKA activation. The recovered 2007 purified-enzyme experiment instead measures PKA inhibition, and PKC effects depend on the tested phosphorylation sites and preparation.
Human CTPS1 forms homotetramers and regulated stacked-tetramer filaments. In the substrate-associated preparations, polymerization enhances activity; H355A retains tetramers and residual activity. This does not make every cellular filament active or polymerization obligatory for every catalytic event. The bacterial filament state differs from the human state tested in PMID:28459447. PMID:34583994 compares the CTPS1 and CTPS2 paralogs; its use of “isoforms” is not evidence about the official CTPS1 splice product. The compact nucleotide-synthesis core uses the existing de novo CTP biosynthesis term, without a redundant additional biosynthesis core.
A separate catalytic role is protein asparagine deamidation. PMID:40240600 uses human HeLa-derived CTPS1 cDNA, purified HEK293T Flag-CTPS1 and bacterial H1.4, with catalytic mutants and direct biochemical endpoints. H1 N76/N77 deamidation permits subsequent EP300 acetylation and chromatin relaxation during DNA repair. CTPS1 performs deamidation; EP300 performs acetylation. PMID:39719712 establishes an IRF3 substrate context, including human endogenous HEK293T/THP-1 perturbations and mouse genetic experiments. The expression-plasmid accession is not specified sufficiently to relabel every recombinant experiment as human IDA. The mouse donor evidence and human cellular corroboration remain distinct. These two substrate contexts support one broad deamidase core with explicit H1 and IRF3 mechanisms, alongside the already present H1-specific annotations.
Official P17812-1 is 591 residues. The single official VSP_055827 deletion removes residues 1–231, giving P17812-2 at 360 residues; both reconstructed sequences equal the separately retrieved official FASTAs. Canonical biochemical experiments do not establish equal nucleotide-synthesis, deamidase or filament activity for the short product. The patient exon-18 lesion, engineered E161K/H355A substitutions and engineered 1–558 construct are also distinct from that official splice product.
The genuine author manuscript for PMID:24503052 was read through its main Methods, Results and Discussion; Figure 5 was visually inspected. Human CTPS1–GFP in HeLa cells supports nuclear and cytoplasmic cytoophidia. Mouse live-imaging constructs elsewhere in that paper are separate. The recovered indexed original for PMID:25223282 includes human MCF7 and HEK293 experiments despite its fly-oogenesis emphasis. Wild-type/E161K localization and fly rescue do not establish every-product equivalence.
The membrane HDA assertion from PMID:19946888 remains UNDECIDED. Its complete abstract includes integral and transiently associated proteins, and the GO membrane definition allows attachment; lack of a transmembrane segment is not a refutation. The target-specific table and full Methods could not be recovered. Conversely, the genuine six-page PMID:7981751 original was recovered and its full scientific text and table captions read. Its drug-resistance experiments use hamster WT/mutant CTPS cDNA in CHO cells, with a human sequence comparison. The existing TAS is retained as a conserved, non-core enzyme/drug-resistance context, not a direct human construct result or general detoxification activity.
Activated T- and B-cell proliferation is supported by CTPS1-specific human deficiency and complementation in PMID:24870241, in addition to the less isozyme-specific PMID:8530356 abstract. These existing process assertions are retained as contextual roles of catalytic nucleotide supply. They do not assign receptor-proximal signaling to CTPS1.
All five generic binding assertions concern CTPS2, an experimentally established CTP synthase. Exact BioPlex, HuRI, OpenCell and the 2025 U2OS AP-MS source records establish the positive pairs. They are refined to enzyme binding without assigning CTPS2 catalytic activity, regulation or a fixed heteromer stoichiometry to CTPS1. Lysate copurification is not described as purified binary binding. The actual OpenCell CSV row is 6465; the actual U2OS NDEx edge is 605930. The 2025 publisher correction concerns a loss-function equation, not the measured interaction. Positive self-association records remain separate and agree with human homotetrameric structures.
The retrieved PTHR11550 topology contains 570 nodes; the target MSA reproduces the 591-residue sequence exactly. All six IBA terms have actual matching IBDs at PTN000167473 or PTN000167476 on the human path. Neither a small donor set nor target self-evidence is a failure. The pyrimidine-nucleobase assertion is refined to CTP biosynthesis because the measured product is a nucleotide. This corrects chemical scope without alleging bad node placement or claiming to have read the yeast donor original. The current donor collection has 332 complete records and 39 exact term/donor joins; the Arabidopsis source alias is preserved and independently resolved against the actual family leaf.
All 151 current ARBA condition sets were evaluated literally. ARBA00029048 matches human branch 17 (zero-based). ARBA00089001 currently has no human match because its taxonomic condition is Saccharomycotina; this version difference remains explicit, while the aggregated activity assertion is independently supported by its other sources and human experiments. GO:0090407 has an organophosphate label/children but a definition mentioning deoxyribose phosphate; CTP biosynthesis is the precise replacement, and the ontology inconsistency is raised as a question.
The Reactome chain R-HSA-73647 → catalyst 73537 → tetramer 504052 → CTPS1 73536 identifies four copies of P17812 residues 1–591 in the cytosol. CTPS1 is the catalyst, not an input. GO-CAM 682fbcd000000000 assigns CTPS1 H1 deamidation and EP300 subsequent acetylation. GO-CAM 682fbcd000000032 assigns CTPS1 deamidase activity and IRF3 transcription-factor activity; PMID:36603579 belongs to the IRF3 node, so it is not a miscited CTPS1 experiment. Both model sources and the index remain byte-exact.
The canonical chemistry consultation independently read the operative PMID:17189248 PDF and selected original Methods/Results for PMID:17463002, PMID:28459447 and PMID:34583994; bounded recovery of PMID:16179339 failed. The deamidase consultation independently read selected full primary Methods/Results for PMID:40240600 and PMID:39719712 and reconstructed the model roles. Owner reads, raw assay/phylogeny/rule reconstruction and exact access limits are recorded separately in the immutable audit ledger. The first full draft is preserved. The subsequent 25-leaf correction adds the structured term-scoping assessment at IBA row 34 and improves scientific wording and spacing; all source objects, actions, products, cores and quotations remain unchanged.
The xenobiotic-response TAS is now marked over-annotated. The original hamster experiments establish mutation-mediated drug resistance and altered CTP feedback regulation, rather than a performed human CTPS1 xenobiotic-response process. CPEC triphosphate is the direct CTPS inhibitor specifically identified in the paper; this claim does not extend to ara-C and 5-FU. The proposed effect of the regulatory mutations on CPEC binding was not directly measured.
The five CTPS2 associations remain enzyme-binding refinements. Their support includes literal human-pair yeast two-hybrid records, as well as separate co-purification datasets. GO:0019899 specifies a catalytic-protein partner class; it does not transfer that partner's activity, require enzyme regulation, or rule out paralog co-assembly. No CTP-synthase-specific binding child was present in the inspected definition and child list. The screen-specific methods remain in the individual reasons; a mechanistic heteromer is not inferred from them.
The catalytic core now uses CTP biosynthetic process, matching the four existing refinements and avoiding an additional upstream-route claim from assays beginning with UTP. The three broader ancestor mappings remain positive source assertions refined to this product-specific process. The separate nucleobase-versus-nucleotide chemical-object issue is unchanged. The actual captured QuickGO definition for GO:0090407 mentions deoxyribose phosphate despite its organophosphate label and broad descendants; its public source is recorded below rather than treated as an unverified memory.
The T-cell-proliferation IDA remains non-core with explicit curator deference. Later CTPS1-specific experiments establish the biology independently, without claiming to resolve the paralog measured in the earlier abstract-only source. Chromatin in the deamidase core describes the H1 substrate context; no additional subcellular site of the IRF3 deamidation reaction is asserted. All source objects, both products, references, original excerpts and prior notes remain unchanged.