The seed7 ordinary hosted fetch supplied the human ANK1 record (HGNC:492, UniProt:P16157), 61 GOA rows and 60 distinct seeded annotation objects. All 60 source objects are preserved, including their evidence types, source identifiers and partner sets. The 23 alternative-product records are unchanged. Their names do not authorize assigning new tested-isoform fields to existing rows. Root imported the exact seed and selected normal auxiliary records; seven pre-existing Reactome records were retained without overwriting. All 14 cited PMID and nine Reactome records are now present. Actual import provenance is retained in tmp/seed7-canonical-import-receipt.json and tmp/seed7-selected-auxiliary-import-receipt.json.
An ordinary just deep-research-falcon human ANK1 --fallback perplexity-lite invocation used the installed client and workspace UV directories. Falcon reached authentication but failed; the fallback failed DNS. The finite attempt ended after 5.85 seconds and produced no provider report. The receipt and sanitized logs are under tmp/ANK1-initial/. These are manual research notes, not an authored provider report.
Ankyrin-1 physically links membrane proteins to beta-spectrin in the erythrocyte membrane skeleton. The original human biochemistry distinguishes spectrin binding to ankyrin-linked band 3 from free band 3; this establishes an adaptor mechanism rather than a generic binding claim [PMID:379653, “Spectrin binds to solubilised ankyrin-linked band 3, but not to free band 3.”]. Human hereditary-spherocytosis variants support the physiological importance of this linkage, but disease association alone is not treated as a new functional assay PMID:8640229. The native erythrocyte complex study independently defines partner interfaces and membrane-protein clustering PMID:35835865.
The gene produces large erythroid and neuronal products as well as short muscle proteins with distinct N-termini. The alternative muscle promoter paper uses human sequence and human muscle immunoblotting; its predicted 155-residue product is not the full-length spectrin-binding erythroid protein PMID:9430667. Small ank1.5/ank1.9 products associate with obscurin and the M-band region, consistent with a sarcoplasmic-reticulum attachment mechanism. Their historical names are retained as reported, without silently mapping ank1.9 to a current human UniProt product PMID:16962094.
For PMID:12354383, the normal abstract and indexed publisher Results/Methods were read. The binding assay uses human erythrocyte AnkR; human lymphocyte complexes contain an AnkR-reactive protein. This supports the CD45 interaction while distinguishing purified binding from cellular association. Direct publisher opening failed, so a complete full-text or supplement reading is not claimed. Original publisher article
For PMID:12409278, the normal abstract plus indexed publisher Introduction/Results/Discussion specify an AnkG190-selective antibody in rat kidney and canine MDCK experiments. Those inspected experiments do not establish ANK1 basolateral localization. The ANK1 row remains unresolved because this assessment does not exclude other evidence or an ANK1 pool in that compartment. Original publisher article
The normal extracted body was read for relevant Methods, Results and Discussion. Ankyrin-R and ankyrin-G shRNAs are distinguished. Human HEK293F, canine MDCK and monkey COS7 hosts are used in different assays; rat Na,K-ATPase constructs and human erythrocyte ankyrin-R add-back are separate reagents. The paper's Methods and Results describe the semipermeabilized-cell system differently, so no single host identity is invented to reconcile them.
Cargo carrying the ATPase ankyrin-binding segment acquires ankyrin-dependent ER-to-Golgi transport. Ankyrin-R depletion impairs selected cargo, and purified human erythrocyte ankyrin restores transport. This supplies a physical cargo-adaptor role rather than only a necessity phenotype. The engineered VSV-MAB chimera reaches Golgi but does not behave like native cargo in stable surface accumulation; its trafficking is not generalized to all plasma-membrane proteins. No supplemental-movie reading is claimed PMID:18768923.
The complete abstract and targeted normal full-body Methods/Results were read. Native human and mouse erythrocyte ankyrin-R is hydroxylated, and recombinant human D34 repeats are tested in separate expression and biochemical systems. FIH/HIF1AN performs the chemistry; ankyrin-R is the substrate. The fragment's stability and band-3 interaction change after hydroxylation, but these observations do not make ANK1 an oxygenase or a demonstrated FIH inhibitor. The real enzyme interaction is retained outside the compact structural core PMID:21177872.
The normal full-body native-complex purification methods, partner-interface Results and relevant Discussion were read. The material is isolated from human erythrocytes. Ankyrin-1 directly organizes membrane partners, including RhCE, band 3, protein 4.2 and a subset containing AQP1. Observed interfaces are distinguished from an inferred autoinhibitory transition. A possible gas-transport metabolon is a proposal about coordinated partner function, not a catalytic activity of ANK1. The source does not justify rewriting the older RhAG-tail interaction as an error PMID:35835865.
The actual local interpro/panther/PTHR24123/PTHR24123-paint.tsv records the six relevant IBDs at PTN002380879: plasma membrane, neuron projection, cytoskeletal adaptor activity, spectrin binding, transmembrane transporter binding and protein localization to plasma membrane. The slice is source evidence for those node assertions; the full tree and MSA were not reconstructed. ANK1's inclusion among experimental descendants is legitimate grounding, and a short donor list is not weak evidence. Target biochemistry independently corroborates the main molecular functions. Broad neuronal localization is retained outside the compact erythroid/muscle core.
The narrower electronic localizations cite rat UniProt A0A8I5ZJ94 and Ensembl ENSRNOP00000076708. One bounded attempt to retrieve the donor failed DNS. Sarcoplasmic-reticulum and M-band assertions have independent small-muscle evidence; Z-disc, A-band, sarcolemmal, axolemmal and postsynaptic-membrane assertions remain unresolved because their original donor experiments were not recovered. These uncertainties do not assert that the source is a wrong paralog or that human ANK1 lacks neuronal activity.
InterPro IPR000488 in the actual UniProt record is the death domain. It is not treated as proof of apoptosis or enzyme catalysis. A broad contextual signaling role is retained from the CD45-associated scaffold, separate from the compact membrane-skeleton core. The nine complete Reactome cached event summaries inform cytosolic location; their reaction names do not assign enzyme activities to ANK1.
The official GO:0008093 definition and parents were checked. Bringing membrane-associated components together with cytoskeletal proteins is consistent with cytoskeletal adaptor activity. Official GO term
No ANK1/P16157 match was found in the cached gocams/index.tsv. No NEW process is proposed. The single core combines cytoskeletal adaptor activity, cytoskeleton organization and plasma-membrane protein localization, without repeating ancestor/descendant process terms. Binding-partner species, host-cell species and tested splice products remain distinct.
All 60 source objects and 23 alternative products are preserved. The draft has 42 ACCEPT, six MODIFY, four KEEP_AS_NON_CORE and eight UNDECIDED decisions, with zero NEW annotations. The six refinements subsume generic structural/binding assertions into already-seeded informative terms. Independent all-row consultation, final checks and a new history record remain pending at this checkpoint.
Independent annotation-reviewer consultation considered all 60 authored rows, core synthesis and preserved source objects. It supported the decisions and requested stronger direct evidence attachments for obscurin binding and the sarcoplasmic-reticulum location; both were added as exact cached excerpts. The final review is COMPLETE with 42 ACCEPT, six MODIFY, four KEEP_AS_NON_CORE and eight UNDECIDED, no NEW rows, one core and all 23 alternative products preserved. The eight scientific uncertainties do not represent missing normal caches.
Final gene validation passed, including term branches, source coverage and citation checks, and HTML rendering succeeded. The 68 supporting-text attachments are exact cached substrings; all 25 raw seed/source files are unchanged. One nonblocking same-term action warning remains: the enzyme-binding IPI concerns ANK1 as an FIH/HIF1AN substrate and is non-core, while the generic enzyme-binding TAS is refined using independent ATPase-binding evidence. Different partners and roles justify the different actions; this is not a preference for an evidence code. The official GO page currently uses the adaptor label, while the local validation ontology uses its anchor label for GO:0008093; authored fields follow the validator label and every original source term label is preserved.
Independent consultation receipt: tmp/ANK1-initial/independent-annotation-consultation.json (SHA256 49fd8e648faad86394068888ba20d38238a76932e7c909a8f20cb647c68213ee). A new scaffolded history record accompanies the review. No Git, remote or shared source-cache writes were performed by the annotation author.
The complete current-head formal review and issue comment were read from the parent-retrieved API response at tmp/ANK1-pr3332-followup/full-pr-review-response.json; pagination is complete and there are no review threads. The published YAML, notes, HTML, raw records, history and reference bytes were copied to an immutable follow-up baseline before editing. Reviewer suggestions are evaluated against the source and project instructions: UNDECIDED remains valid for genuine uncertainty, and an abstract-only cache is not a complete paper.
For PMID:1833445(https://www.researchgate.net/publication/21323428_Immunocytochemical_localization_of_fodrin_and_ankyrin_in_bovine_chromaffin_cells_in_vitro), the original paper's textual Methods, Results and relevant Discussion through the conclusion were read in an author-uploaded copy, with title and DOI matched to the normal record. Image pixels were not independently inspected. Rat erythrocyte ankyrin immunogen, bovine chromaffin cells, microtubule-absorption controls and 215-kDa immunoreactivity are explicit. The study maps antigen to filaments and coated membrane; granules were largely lost during unroofing. It leaves functional significance open and discusses secretion versus membrane retrieval. The official exocytosis definition concerns vesicle preparation/fusion and release. A source-specific overannotation assessment is therefore being considered on the actual experiment's inferential scope, without declaring the bovine antigen a different gene or denying independently supported cargo trafficking. The original normal cache remains abstract-only and unchanged.
For PMID:12409278(https://journals.physiology.org/doi/full/10.1152/ajprenal.00100.2002), indexed primary Introduction and Results explicitly name an antibody to the unique N-terminal sequence of AnkG190. Rat-kidney and canine-MDCK immunoblot controls and basolateral staining are described. This is stronger source-identity evidence than the abstract's generic phrase about a kidney-specific isoform. The basolateral membrane definition is spatial, and these inspected experiments identify the stained reagent. A source-specific overannotation assessment does not assert that ANK1 can never occupy that compartment. Direct publisher opening failed, so this remains targeted indexed body access rather than a claim to the entire paper or supplements.
Eight exact missing PMID records received one ordinary fetch batch in an isolated tmp directory. It timed out after 45 seconds with exit -15 and produced no output. This is one batch timeout, not eight individually completed failures. Exact identities and actual read scopes are in tmp/ANK1-pr3332-followup/additional-primary-assessment.json; normal cache recovery is pending. No substitute publication or provider files were authored.
The official Z-disc, A-band and axolemma definitions and parents were inspected. A band includes M band by a part-of relation, correcting any implication that the two are anatomically unrelated. Regional staining, physical membrane pools and structural sarcomere membership require distinct explanations. Candidate articles encountered only as titles/bibliography, including PMID:9727010, the 2025 sAnk1 juxtamembrane study, the Purkinje-survival study and the beta-III-spectrin dendritic study, have not been used for new claims or treated as fully consulted sources.
The eight normal records are now present and unchanged after the parent imported the verified Source30 artifact. All eight canonical records were compared byte-for-byte with the strict staging copy and exact ZIP member. Five records contain extracted full text (9024692, 22045734, 25362473, 26405035, 34180393); three remain abstract-only (2139035, 9664041, 16308276). The finite scientific assessment is tmp/ANK1-pr3332-followup/source30-actual-source-assessment.json. A full-text flag describes extraction availability, not a claim that every figure, supplement or duplicated XML paragraph was inspected.
For PMID:9024692, the full main Methods, Results and Discussion now distinguish rat large Ank1 at the sarcolemma from small Ank1 in internal SR membranes. Antibodies against different Ank1 regions yield distinct immunoblots; loss of the large sarcolemmal signal in nb/nb mouse muscle supports its gene assignment. Rabbit SR fractions enrich the small forms. The HEK293 expression experiments use rat small-Ank1 cDNA, not a human reagent inferred from the host. The small forms align with Z and M levels, but the paper explicitly says they surround myosin at the M-line level rather than forming integral M-line proteins [PMID:9024692, “Thus, the small ankyrins are not integral to the M lines but instead appear to surround the myosin filaments at the level of the M lines.”]. This supports the SR pool and warns against equating any axial alignment with structural membership of a sarcomeric disc.
The complete available main body of PMID:22045734 identifies primary flexor digitorum brevis fibers from adult rats, in both Methods and Results. The prior identity-assessment note repeated the later 2015 paper's description of those fibers as mouse; the actual 2011 Methods resolves that discrepancy. siRNA targeted to the short-isoform 5′ UTR disrupts network SR, reduces SERCA/sarcolipin protein without reducing their mRNAs, and leaves several sarcomeric markers comparatively intact. Rescue restores SERCA distribution. This strengthens a distinct SR-maintenance role without proving a Z-disc constituent or manufacturing a new biological-process annotation [PMID:22045734, “Our results show that sAnk1 stabilizes the nSR and that its absence causes the nSR to fragment into distinct membrane compartments.”]. Figure-image pixels and supplements were not independently read.
The complete main Results, Discussion and Methods of PMID:25362473 resolve neuronal gene identity using mouse Ank3 conditional deletion and Ank1 pale genetics. AnkR occupies developing PNS nodes and compensates at nodal membrane after AnkG loss; mature control nodes have less AnkR, and developing CNS nodes rarely show the same enrichment. Antibody controls include AnkR-deficient tissue. These observations support a conditional/developmental axolemmal pool and neuronal projections, without making AnkR the principal constitutive adult nodal ankyrin. Methods explicitly identify full-length Flag/GFP-AnkR and its membrane-binding-domain reagent as human sequence. The tissue observations remain mouse observations. Historical PMID:2139035 erythroid-reactive antibody staining is supportive context, not the decisive modern gene-identity evidence.
PMID:34180393 was read for neuronal localization, knockout antibody controls, beta1-spectrin association, Kv3.1b recruitment and their figure legends, plus the entire main Methods and Discussion. Human cortical biopsies show membranous AnkR in subsets of interneurons and colocalization with Kv3.1b. The mechanistic genetics are mouse experiments. This is evidence for a neuronal membrane role, not evidence for a postsynaptic compartment from soma staining alone. The Methods cite Ho2014 for AnkR-GFP; an indexed resource table labels it mouse while Ho2014 explicitly says human. That unresolved reagent-description conflict is retained, so no species-specific new recombinant activity claim is based on the conflict. Other Results, source data, image pixels and supplements were not exhaustively reviewed.
The entire available main body of PMID:26405035 supports direct sAnk1–SERCA1 association and reduced apparent SERCA1 calcium affinity in the tested systems. Native SR and SERCA1 cDNA are rabbit; COS7 is the expression host. The sAnk1 construct comes from a cited earlier vector and its species is not explicitly assigned in this Methods section. A list of human/mouse accessions and human structural-modeling inputs does not resolve the assayed construct's identity. No new human SERCA-regulator annotation is proposed. PMID:16308276 remains abstract-only in the normal cache; its membrane-integration and orientation evidence supports the SR assignment, but full Methods and reagent species remain unverified.
The bovine chromaffin study maps ankyrin-reactive antigen to filaments and coated membrane and leaves secretion versus membrane retrieval unresolved. This original-body observation, documented above with the author-uploaded primary URL, supports a source-specific overannotation assessment of exocytosis; it does not identify the antigen as a different gene. The renal study's inspected primary body identifies an antibody to the unique AnkG190 N-terminal sequence, including the 15–31 region. This reagent-specific evidence supports a source-specific overannotation assessment of the ANK1 basolateral NAS row, without a claim that ANK1 is excluded from basolateral membranes in every context. Both normal caches remain abstract-only and unchanged. These two judgments received independent original-paper consultation.
Four transferred locations receive positive independent support and are retained as non-core: sarcolemma from the distinct large Ank1 pool and nb/nb controls; axolemma from genetically resolved developmental/compensatory nodal AnkR; and A-band and Z-disc regions from the comparative rat muscle study. The A-band definition includes the M band, so the previous suggestion that M-band localization cannot inform this region was too categorical. The broad A-band assignment is retained in its regional sense, not as evidence for a separate thick-filament catalytic or structural activity. The original rat donor chain remains unreconstructed; independent evidence supports these locations without pretending to have recovered that chain.
Z-disc is retained as a non-core regional localization after independent consultation challenged an inconsistent standard between Z and M bands. The comparative rat study reports a thin AnkR-positive band colocalizing with alpha-actinin at Z lines, beyond the separate small-Ank1 SR pool that surrounds Z/M levels. This supports the existing located_in assertion without claiming that all small Ank1 is an integral structural constituent of the actin-anchoring plate. The accepted M-band assertion likewise has small-isoform/obscurin colocalization evidence and is retained with its peripheral M-band-region scope; it is not converted into a thick-filament-crosslinker claim. Postsynaptic membrane remains UNDECIDED because the comparative 1998 paper itself allows antibody cross-reaction with low-abundance subsynaptic AnkG480. Neither broad brain expression nor human somatic membrane staining resolves that particular compartment. Epithelial apical/basal polarity also remains UNDECIDED: selective cargo transport is established, but the relevant family-review experiment for overall polarity remains unavailable.
The optional suggestions were assessed separately. The ATPase-binding MODIFY retains a source-level refinement to a term already present; it creates no new independent function. FIH/HIF1AN binding remains non-core because the assay establishes a genuine enzyme–substrate interaction and the GO enzyme-binding term does not require regulatory activity; ANK1 is not called an FIH regulator. Obscurin binding remains a cytoskeletal-adaptor refinement, now explicitly a membrane-to-cytoskeleton anchoring model supported by binding, SR targeting and independent SR-maintenance evidence, rather than a claim that the interaction alone proves the entire maintenance mechanism. A separate short-muscle core describes that distinct architecture and SR site, without duplicating the erythroid ankyrin complex there. The description now refers to isoforms rather than a gene family. Neuron projection receives direct axonal evidence. Repeated Reactome location reasons are shortened while preserving the distinction between a family-containing event and an ANK1-specific enzymatic mechanism.
No NEW annotation or process is added. All 60 original source assertions, qualifiers, partners and 23 alternative products are preserved. Independent final consultation and validation are recorded in the new follow-up history; the original published history is untouched.