This guide distinguishes actual selected original text or target tables from curated interaction records, abstracts and bibliography-only sources. It now accompanies genuine native acquisition and exact reconciliation of 73 original contexts, all 16 TSV columns and 73 native seed objects. The accepted scientific assessment has been applied to the genuine seed; validation and publication status are recorded separately in the notes. Normal cache availability must not be confused with access to separately retained originals. Five short, literal snippets from immutable normal caches now anchor specified iron-handling, structural and receptor-contact claims; their source locations and limits are recorded in the evidence archive.
Human L-chain shells and H/L heteropolymers support iron incorporation, mineralization and storage. Human deficiency/rescue demonstrates composition-dependent homeostasis. These are distinct from rapid catalytic oxidation at H-chain ferroxidase centers. Ferritin is autophagic cargo; receptor association, turnover and cargo necessity do not automatically make FTL autophagy machinery. The observed 2014, 2015 and 2019 variant effects remain study-specific.
The retained PTHR11431 tree places the exact 175-aa human sequence at AN31/PTN002478947. All three incoming IBA terms join positive AN0/PTN000153092 IBDs with matching descendants. A target appearing in the cytoplasm donor set is valid grounding. Cytoplasm is more general than the retained cytosol location via part_of; this scope decision does not reject its node placement.
Preserved official UniProt bibliography records this source for nucleotide sequence [mrna] of 33-175. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Preserved official UniProt bibliography records this source for nucleotide sequence [genomic dna]. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Preserved official UniProt bibliography records this source for nucleotide sequence [mrna]. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Preserved official UniProt bibliography records this source for nucleotide sequence [mrna]. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Preserved official UniProt bibliography records this source for protein sequence of 2-36 and 41-175; cleavage of initiator methionine; acetylation at ser-2. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Authentic abstract concerns an FTL regulatory/clinical hyperferritinemia-cataract context. Homeostasis and ferritin membership are independently established; this source is not presented as a newly verified shell-assembly assay. Full original Methods were not read.
Authentic abstract concerns iron-responsive-element regulation and hyperferritinemia/cataract. This is relevant regulatory context, not an independently verified direct protein iron-binding assay. The gene-level iron-binding decision relies on separate biochemical studies; full original Methods were not read.
Preserved official UniProt bibliography records this source for protein sequence of 84-90 and 145-155. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Preserved official UniProt bibliography records this source for nucleotide sequence [large scale mrna]. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Preserved official UniProt bibliography records this source for nucleotide sequence [large scale genomic dna]. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Preserved official UniProt bibliography records this source for nucleotide sequence [large scale mrna]. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Preserved official UniProt bibliography records this source for variant nbia3 thr-96. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Authentic abstract describes a human ORF Y2H matrix. Exact source-qualified IntAct entries support FTL–FTH1 and self-association. Original target supplementary rows and target-specific pull-down validation were not reread; network-wide validation is not assigned to each pair.
Authentic abstract describes the human CCSB-HI1 Y2H map; exact source-qualified IntAct entries identify FTL–FTH1 and self-association. Target supplementary rows and target-specific orthogonal assays were not independently read. Positive assembly evidence is retained without a native stoichiometry claim.
Authentic abstract, author-deposited PDB 2FG4/2FFX metadata and indexed Figure 3 caption support recombinant human L-chain ferritin assembly. Full article Methods returned an access failure. Crystallographic cadmium is not an iron-oxidation assay or proof of H-like ferroxidase activity.
Original Methods pages 83–84 and Results/Figure 4 caption page 87 were read as text. The MOST1 screen recovered an FTL fragment; tagged proteins expressed separately in hamster BHK cells were mixed as lysates for reciprocal co-IP. This is not an endogenous human cancer complex, a full-length FTL screen construct or a measured mitogenic FTL function.
Preserved official UniProt bibliography records this source for nucleotide sequence [large scale mrna]. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Selected indexed original Methods 2.3, Table 1 and Figure 1 text were read despite direct-page/full-body access failures. Human FTL 1–175 was identified and reciprocal NAMPT/PBEF association tested in human pulmonary endothelial cells. NAMPT perturbation/ROS endpoints do not assign FTL oxidase activity.
Actual original Results/Table 1 and Concise Methods identify FTL (Pep5/ID14) in a purified pooled human urinary exosome fraction. The literal urine extension is retained. Detection does not establish uniform vesicle occupancy or a role in exosome biogenesis; no raw-spectrum audit.
Preserved official UniProt bibliography records this source for variant hrftc ile-30. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Selected indexed original iron-incorporation Results and Figures 1, 5 and 6 were read. Recombinant human wild-type L-chain homopolymers incorporate iron; a neuroferritinopathy frameshift impairs incorporation and competition. No complete XML body, all supplements or H-chain-like FTL active-site catalysis is claimed.
Authentic abstract describes human YTS NK-like membrane proteomics, but full Methods and the exact FTL target row were not recovered. Membrane includes attached proteins, so lack of a transmembrane helix does not refute the HDA claim. Source-specific FTL localization remains unresolved; no wrong-gene allegation.
Selected indexed original recombinant H/L Methods and iron-oxidation Results/Figure 6 were read. Mutant L chains alter incorporation and permeability while H-containing ferroxidase kinetics distinguish catalytic H centers from L-chain shell effects. Complete original XML body and all supplements were not recovered.
Preserved official UniProt bibliography records this source for identification by mass spectrometry [large scale analysis]. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Actual original Y2H/PCA/wNAPPA Methods and publisher Supplementary Table 2 were read. PDF page 13 explicitly contains FTH1–FTL Entrez 2495–2512, with human ORFeome proteins in a yeast assay. Target-specific PCA or cell-free wNAPPA positivity is not specified by this pair list; the general PCA host is CHO-K1.
Selected original Methods 2–4/7 and Results 11/Figure 3 caption were read. HTT bait is residues 1–506; source-qualified IntAct reports FTL Y2H and LUMIER contexts. Original target supplementary row was not reread, and no full-length endogenous HTT interaction or disease-modifier mechanism is inferred.
Actual main Methods/Results describe human expressed-prostatic-secretion urine fractions and possible nonvesicular carryover. Exact FTL Supplementary Table 2 remains unverified after challenge responses. Independent PMID:19056867 supports the unrestricted exosome location; no prostate-specific FTL mechanism is inferred.
Actual original Methods/Results/Discussion and Figures 1–4 captions were read. An initial PEN2 loop 34–65 screen is separate from reciprocal full tagged human FTL/PEN2 co-IP in HEK293 cells. PEN2/PS1 abundance effects support contextual association but do not measure FTL protease activity or degradation kinetics.
Selected original patient-fibroblast Results and transduction, 55Fe, immunoblot and pulse-chase Methods were read. Loss of detectable L chain with retained H chain increases sequestration and lowers labile iron; wild-type L rescue partially restores availability. The undetected patient truncation is not a documented natural product.
Preserved official UniProt bibliography records this source for identification by mass spectrometry [large scale analysis]. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Selected original main-text AP-MS, ferritin localization and NCOA4 perturbation/rescue passages were read. FTL-containing ferritin is receptor-selected cargo. Co-complex enrichment and cargo delivery do not identify direct FTL–NCOA4 contact or make FTL autophagy machinery; complete Methods and target supplementary rows were not all read.
Authentic abstract and original Supplementary Figures 2/4/5/6 captions were read; complete main Methods and detailed subunit-localization panels were not recovered. Human DLD1 NCOA4 pulldown enriches FTL/FTH1, while re-expression distinguishes FTH1-specific contact. Ferritin is cargo; the corresponding incoming annotation describes autolysosome localization, not participation in an autophagy process.
Selected original Results 3, Methods 10 and dataset description 16 were read. Human ORF Y2H uses quadruplicate retesting and sequence confirmation. Exact target Table S2G contexts are retained curated IntAct records; original FTL supplementary rows and target-specific orthogonal validation were not independently reread.
Original selected Methods/Results and Table S2 rows 62–65 with its explicit legend were read. FTL Q26L/A27V/T30I/A96T have GFP1 and Y2H1, indicating stable/no disruption in this study. Later 2019 source-specific calls differ; neither those later calls nor generic IntAct feature labels overwrite these original values.
Original main Results S5 and Methods S13, supplement 8 Y2H methods/legend, and supplement 11 Table S3A rows 960–967 were read. WT FTH1–FTL and FTL–FTL are positive; FTL A96T/H133P lose tested interactions. The complete S3B target scan has no FTL/FTH1 GPCA rows. Human proteins are assayed in yeast; no natural-isoform or purified-affinity claim.
Preserved official UniProt bibliography records this source for identification by mass spectrometry [large scale analysis]. The original paper and target-specific findings were not independently consulted in this assessment; this metadata-only entry supplies no additional functional, product or localization assertion.
Selected original author-PDF Results/Experimental Procedures and Figure 2/4 captions were read. Mouse NCOA4 knockout and prolonged low iron affect erythroid iron supply; untreated terminal differentiation is substantially unchanged and ferritin assays detect FTH1. This does not isolate FTL-specific differentiation, so that original NAS claim remains unresolved.
Original Methods 1–3 were read: sequenced human HA-FLAG ORFs, anti-HA AP-MS and CompPASS-Plus filtering. Exact FTL–FTH1/NCOA4 contexts are source-qualified IntAct records, not independently reread target SI. Recovery supports co-complex association without resolving direct contact or subcellular localization.
Authentic abstract includes FTL/FTH1 expression and prognostic findings in acute myeloid leukemia. Identifier and relevance are supported, but source-specific NAS assembly/homeostasis mechanisms were not independently verified from full text. Separate human functional studies support those gene-level capacities.
Selected original Methods/Results, exact Supplementary Data 2/4 target rows and numeric coding were read/replayed. Data 2 contains non-disruptive FTL-related contexts; Data 4 calls Q26L/A27V/T30I/A96T disruptive, with coding independently matching published cohort totals. This differs from 2014 S2 but does not erase positive WT baselines or establish universal variant effects; no FTL-specific PCA result claimed.
Original HuRI assay-design/validation Results were read: three Y2H versions, quadruplicate verification and sequence confirmation. Exact FTL pairs are supported by retained source-qualified IntAct records. Original target Table 9 rows and target-specific orthogonal or structural validations were not reread.
Selected author-PDF target-selection and Y2H/DULIP/LuTHy Methods were read. Exact partners, isoforms and construct ranges come from source-qualified IntAct records; original FTL Table S2 rows were not reread. HTT fragment boundaries and unspecified ATXN1 construct limits remain explicit. No automatic mammalian validation or disease-modifier role is assigned.
Original BioPlex3 limitations, clone construction, stable-cell, affinity, scoring and network-assembly sections were read. Human tagged ORFs in 293T/HCT116 generate gene-level AP-MS associations; exact FTL contexts are curated IntAct records. No target SI reread, purified contact, isoform-specific function or compartment inference.
Actual original Results sections 3–6, selected Methods 8/11/13/14/17, Figures 1–5 captions and Table 1 were read. Human wild-type FTL and engineered L2H are assayed; productive receptor contact is assigned to FTH1 and gained by L2H. Wild-type relative-IP background is not numerically zero. No transfer of engineered gain to wild-type FTL or complete raw-data/image review.
Selected original AP-MS Methods/Results and the author-linked NDEx CX dataset were read. Exact FTL–FTH1 edge 561950 and FTL–NCOA4 edge 562046 occur in the human U2OS network. This is positive primary co-complex evidence, not direct receptor contact or FTL autophagy machinery.
Actual event and selected entities contain the cytosolic 24-subunit FTH1/FTL ferritin model. Retain cytosolic storage context; complex oxidation is not assigned to the individual L chain.
Preserved official UniProt pathway cross-reference to Scavenging by Class A Receptors. The broad pathway entry and all nested reaction roles were not independently inspected here; it adds no new process or membrane-topology assertion.
Preserved official UniProt pathway cross-reference to Golgi Associated Vesicle Biogenesis. The broad pathway entry and all nested reaction roles were not independently inspected here; it adds no new process or membrane-topology assertion.
Actual event and selected entities include cytosolic FTL-containing ferritin in Golgi-associated handling. The starting cytosolic location is supported; integral membrane topology and a new secretion mechanism are not inferred.
Preserved official UniProt pathway cross-reference to Neutrophil degranulation. The broad pathway entry and all nested reaction roles were not independently inspected here; it adds no new process or membrane-topology assertion.
Actual event and selected physical entities include human P02792 residues 2–175 in azurophil-granule lumen and extracellular output sets. This supports contextual release/localization, not a newly read underlying assay or the principal ferritin activity site.
Preserved official UniProt pathway cross-reference to Iron uptake and transport. The broad pathway entry and all nested reaction roles were not independently inspected here; it adds no new process or membrane-topology assertion.
All three incoming IBA assertions join literal positive IBDs at PTHR11431 AN0/PTN000153092 on the exact human AN31/PTN002478947 lineage. Donor sets match, including valid human target self-evidence for cytoplasm. Ferrous/ferric binding remain core; cytoplasm granularity is considered separately. No invented loss or donor-count objection.
Original InterPro inference provenance is retained for ferric binding, iron transport and homeostasis. Independent functional and shell evidence supports the scoped decisions; the family mapping is not relabeled as a new target experiment.
Original mouse P29391 ISS donor is retained. Official current mouse records were examined; autolysosome ISO points back to human P02792 and is not independent mouse IDA. Separate human cargo evidence supports the contextual location without a guessed donor replacement.
Original UniProt subcellular-location inference provenance is retained. Cytoplasm granularity follows the actual cytosol part_of path; autophagic locations describe ferritin cargo destinations rather than execution of the process.
Official human 175-aa P02792 sequence, HGNC identity and family PTHR11431/PTHR11431:SF47 were checked against retained responses. No alternative-product declaration occurs. Engineered fragments, disease variants and old constructs are not added as natural isoforms; the H-chain comparison is functional, not an automatic transfer of catalysis.
PMID25910212: official Table S3 workbook, Table S3A rows 960–967; original supplemental methods/legend, Table S3 legend and pairwise-Y2H methods. The complete S3B target scan finds no FTL/FTH1 GPCA entries.
PMID21516116: publisher supplement, Table 2 heading page 11 and Entrez 2495–2512 on page 13. The target page was visually inspected.
PMID26776506: author repository original, selected erythropoiesis/ferritin-targeting Results, Experimental Procedures and Figure 2/4 captions.
PMID25327288: publisher original, authentic abstract and indexed Supplementary Figure 2/4/5/6 captions; no claim of complete main Methods or detailed localization-panel reading.
PMID19056867: PMC original, Table 1/Results and Concise Methods. PMID23533145: PMC original, main Methods/Results; exact target Supplementary Table 2 remained inaccessible.
All 73 literal originals, their reference identifiers, partner groups, qualifiers and the single urine extension remain exact. The preserved private exporter forecast is now reconciled to the genuine 73-row export and 73-row native seed using explicit physical-line and stored-row locators. The original urine atom is restored in the reviewed annotations, leaving the archived native seed unchanged. No natural alternative product is declared. The 57 manual source assessments include 45 PMID entries, seven Reactome entries, four original GO_REF sources and the official UniProt record; unconsulted bibliography-only sources are explicitly unverified.
All 55 planned normal sources are present: 37 exact existing-main files and 18 native acquisitions. Existing PTHR11431 entries, metadata and the seven-row PAINT slice were retained unchanged; its three target IBD rows match the dated family proof. Cache flags describe the acquired files and do not establish that all original Methods, images or supplements were inspected. The selected-reading limits above remain unchanged, including explicitly unverified bibliography-only sources.
| Source | Cache reports full text | Acquisition |
|---|---|---|
| PMID:14702039(https://pubmed.ncbi.nlm.nih.gov/14702039/) | no | reused unchanged |
| PMID:15057824(https://pubmed.ncbi.nlm.nih.gov/15057824/) | no | reused unchanged |
| PMID:15489334(https://pubmed.ncbi.nlm.nih.gov/15489334/) | no | reused unchanged |
| PMID:16116125(https://pubmed.ncbi.nlm.nih.gov/16116125/) | no | native acquisition |
| PMID:16169070(https://pubmed.ncbi.nlm.nih.gov/16169070/) | no | reused unchanged |
| PMID:16189514(https://pubmed.ncbi.nlm.nih.gov/16189514/) | no | reused unchanged |
| PMID:16790936(https://pubmed.ncbi.nlm.nih.gov/16790936/) | no | native acquisition |
| PMID:17143515(https://pubmed.ncbi.nlm.nih.gov/17143515/) | no | reused unchanged |
| PMID:17974005(https://pubmed.ncbi.nlm.nih.gov/17974005/) | yes | reused unchanged |
| PMID:18486613(https://pubmed.ncbi.nlm.nih.gov/18486613/) | no | reused unchanged |
| PMID:19056867(https://pubmed.ncbi.nlm.nih.gov/19056867/) | no | reused unchanged |
| PMID:19176363(https://pubmed.ncbi.nlm.nih.gov/19176363/) | yes | native acquisition |
| PMID:19923220(https://pubmed.ncbi.nlm.nih.gov/19923220/) | no | native acquisition |
| PMID:19946888(https://pubmed.ncbi.nlm.nih.gov/19946888/) | no | reused unchanged |
| PMID:20159981(https://pubmed.ncbi.nlm.nih.gov/20159981/) | no | native acquisition |
| PMID:21269460(https://pubmed.ncbi.nlm.nih.gov/21269460/) | yes | reused unchanged |
| PMID:21516116(https://pubmed.ncbi.nlm.nih.gov/21516116/) | yes | reused unchanged |
| PMID:23275563(https://pubmed.ncbi.nlm.nih.gov/23275563/) | yes | reused unchanged |
| PMID:23533145(https://pubmed.ncbi.nlm.nih.gov/23533145/) | yes | reused unchanged |
| PMID:23685131(https://pubmed.ncbi.nlm.nih.gov/23685131/) | yes | reused unchanged |
| PMID:23940258(https://pubmed.ncbi.nlm.nih.gov/23940258/) | yes | native acquisition |
| PMID:24275569(https://pubmed.ncbi.nlm.nih.gov/24275569/) | no | reused unchanged |
| PMID:24695223(https://pubmed.ncbi.nlm.nih.gov/24695223/) | yes | reused unchanged |
| PMID:25327288(https://pubmed.ncbi.nlm.nih.gov/25327288/) | no | reused unchanged |
| PMID:25416956(https://pubmed.ncbi.nlm.nih.gov/25416956/) | yes | reused unchanged |
| PMID:25502805(https://pubmed.ncbi.nlm.nih.gov/25502805/) | yes | reused unchanged |
| PMID:25910212(https://pubmed.ncbi.nlm.nih.gov/25910212/) | yes | reused unchanged |
| PMID:25944712(https://pubmed.ncbi.nlm.nih.gov/25944712/) | no | reused unchanged |
| PMID:26776506(https://pubmed.ncbi.nlm.nih.gov/26776506/) | no | native acquisition |
| PMID:28514442(https://pubmed.ncbi.nlm.nih.gov/28514442/) | yes | reused unchanged |
| PMID:3023856(https://pubmed.ncbi.nlm.nih.gov/3023856/) | no | native acquisition |
| PMID:30325535(https://pubmed.ncbi.nlm.nih.gov/30325535/) | no | native acquisition |
| PMID:31515488(https://pubmed.ncbi.nlm.nih.gov/31515488/) | yes | reused unchanged |
| PMID:32296183(https://pubmed.ncbi.nlm.nih.gov/32296183/) | yes | reused unchanged |
| PMID:32814053(https://pubmed.ncbi.nlm.nih.gov/32814053/) | no | reused unchanged |
| PMID:33961781(https://pubmed.ncbi.nlm.nih.gov/33961781/) | yes | reused unchanged |
| PMID:3754330(https://pubmed.ncbi.nlm.nih.gov/3754330/) | no | native acquisition |
| PMID:3840162(https://pubmed.ncbi.nlm.nih.gov/3840162/) | no | native acquisition |
| PMID:3858810(https://pubmed.ncbi.nlm.nih.gov/3858810/) | no | native acquisition |
| PMID:38714719(https://pubmed.ncbi.nlm.nih.gov/38714719/) | yes | native acquisition |
| PMID:40205054(https://pubmed.ncbi.nlm.nih.gov/40205054/) | yes | reused unchanged |
| PMID:6653779(https://pubmed.ncbi.nlm.nih.gov/6653779/) | no | native acquisition |
| PMID:7492760(https://pubmed.ncbi.nlm.nih.gov/7492760/) | no | native acquisition |
| PMID:7493028(https://pubmed.ncbi.nlm.nih.gov/7493028/) | no | native acquisition |
| PMID:8706699(https://pubmed.ncbi.nlm.nih.gov/8706699/) | no | reused unchanged |
The evidence archive now reproduces selected original IntAct fields for 94 source-qualified records covering 28 of the 34 generic-binding contexts. The six remaining contexts have separately identified original-paper support. These are source records and original locators, not additional experiments or repeated review judgments. The dated query URL, response checksum, record indices, exact partners, methods, host organisms, expansion labels and construct features permit the joins to be checked. An absent exact source pair in that query is not absence from the publication.
In particular, the HI-NGS supplement lists FTH1–FTL on PDF page 13; the 2015 original Table S3 workbook distinguishes positive WT pairs in rows 960, 962 and 963 from mutant losses; and the 2025 author-linked NDEx network contains FTL–FTH1 edge 561950 and FTL–NCOA4 edge 562046. Table S3B does not contain an FTL/FTH1 GPCA entry.
All 34 generic-binding original contexts remain positive, contextual associations. None is an FTL self-partner context; the seven incoming identical-protein-binding annotations already describe self-association. Nine generic contexts concern FTH1, with six binary-screen sources and three AP-MS sources. Neither a positive pairwise reporter nor co-complex recovery alone establishes the two-subunit stoichiometry required by protein heterodimerization activity. The ferritin shell structural role is instead synthesized from independent structural and functional evidence.
Iron ion transport explicitly includes movement within a cell through a pore, so ferritin pore-dependent movement is not excluded by the absence of a biological membrane. The two broad experimental iron-binding annotations remain TOO_GENERAL because incorporation, ferrous input, oxidation and mineral retention do not independently isolate a valence-specific L-chain binding event. The retained ancestral Fe(II)-binding assertion is represented in a distinct core function; the shell core uses structural molecule activity. The contributes_to molecular-function slot is not used as a list of additional activities.