The immutable normal intake contains 45 annotations, four products and ten reference identity pairs. All are preserved. The selected main publication bytes are kept unchanged; PMID:18287031 has a genuine full normal variant in the intake archive that was read separately from the main abstract. Three new full rodent studies and two genuine abstracts were fetched through the normal publication tool. The default Falcon attempt timed out, and the single fallback returned an explicit quota error. No provider report was manufactured; these notes record the manual research.
The original human-library experiment identified CNKSR2 as a Densin interactor. Subsequent mechanistic assays used rat MAGUIN-1 fragments with human Densin and PSD-95. Removing the terminal motif or the appropriate self-association region disrupted the relevant contacts; a MAGUIN C-terminal fragment assembled the three-protein complex. The original assay does not resolve a fixed dimer versus a larger oligomer, nor does it demonstrate a full-length human endogenous ternary complex. Current GO:0140378 describes the integral organizing role more precisely than the broad adaptor assertion. The scaffold is the component that performs the assembly work, not an enzyme or a passive substrate PMID:12390249.
A literal MINT metadata discrepancy is retained: positive pair EBI-8548334 assigns Densin residues 1242–1442, which the original paper identifies as the negative PDZ-deleted construct. The actual positive human-library bait spans 1242–1537. The positive interaction and PDZ refinement remain supported by the original experiment and independent target peptide assays; the raw source record is not repaired by hand.
Official UniProt features reconstruct the four products to 1034, 898, 849 and 1004 residues. Products Q8WXI2-2 and -4 omit the terminal 899–1034 segment; -4 also lacks 271–319. Product -5 lacks 435–464 but retains the terminal motif. Exact official ENA translations for the original CNK2A/B cDNAs match current -1/-2. Rat experimental coordinates are preserved as rat coordinates, with an independently recorded alignment. Retaining a sequence motif in -5 does not demonstrate its whole-protein activity. These differences belong in interpretation, while all four machine product objects remain exact.
The human terminal 1025–1034 peptide binds isolated PDZ domains in the fragmentomics study. The 22 source-specific partner groups are refined to GO:0030165, with precise partner ranges and tags in the index. The source measures peptide/domain affinity; it does not prove that every pair forms a native full-length complex. APBA1 includes a residue-655 feature; a separate NHERF4 isoform-2 record is preserved as such, alongside the two exact canonical-partner records PMID:36115835.
The EGFR interaction is independently positive in human-library MaMTH and tagged coimmunoprecipitation, including wild-type EGFR. CNK2 showed similar binding patterns for wild-type and tested oncogenic EGFR variants. The detailed TACC3 cancer mechanism in that paper is not transferred to CNKSR2 PMID:27956147. Human CNK2 binds Raf and Rlf in the positive original abstract, supporting membrane localization and kinase-partner specificity. Full Methods/Results of that 2003 report remained unavailable after bounded legitimate retrieval attempts; neither pathway direction nor a new catalytic role is inferred PMID:14597674.
Human CNK2 and fly HYP SAM fragments form a stable 1:1 complex in the separately preserved full text. This supports heterodimerization at that precise fragment and cross-species scope. The functional fly-cell RAF experiments and the human/fly complex that did not bind fly KSR are distinguished from a native human signaling complex PMID:18287031.
Rat-neuron experiments connect CNK2–Vilse binding to localization and spatial Rac signaling, with wild-type rescue, interaction-site mutants and competitive fragments. The isolated binding fragment did not alter Vilse catalytic activity; Vilse supplies the GAP chemistry. These performed organizing actions support the already-existing postsynapse terms without adding new Rac or spine-development processes PMID:24656827.
The TNIK study uses mouse Cnk2 constructs and rat neuronal preparations. Full-length protein recruits TNIK to membranes in heterologous cells; loss of the C-terminal membrane-association region redistributes the bound kinase. In neurons the effect is smaller, and CNK2 knockdown did not significantly alter dendritic TNIK content. The authors did not establish that altered TNIK explains the PSD-size effect. Endogenous rat imaging separately supports postsynaptic location PMID:32235845.
Mouse Cnksr2 loss reduces postsynaptic PSD-95 signal and AMPA-receptor cluster intensity while leaving cluster density and total surface-receptor abundance distinct from those changes. The mouse MAGUIN/rat afadin construct experiments support a partner-assembly mechanism; they are not human endogenous assays. These results support the existing organization annotations and one integrated scaffold core PMID:36803960. The older rat MAGUIN abstract positively reports cell bodies, neurites, membrane association and brain coimmunoprecipitation PMID:10207009. The mouse phosphoproteomics table for PMID:17114649 remains uninspected, so that exact supporting relationship is UNVERIFIED even though independent neuronal evidence supports the location.
Current mouse, rat, human CNKSR1 and fly identities are authenticated. The original doubled MGI namespace is preserved and explicitly mapped to the official mouse record. Current descendant annotations and experimental sources are separate from the historical PAINT tree and IBD placements, which were not reconstructed. The target's own experimental membrane annotation is legitimate grounding. The mapped fly UniProt records repeat inherited claims; an invalid namespace query is preserved as a failed access attempt and supplies no negative evidence.
The urinary-exosome laboratory database contains CNKSR2/NP_055742 with two peptides under the key for PMID:19056867 and explicitly describes healthy-human urinary samples. This is retained as secondary proteomic localization, not an extracellular mechanism. Earlier PMC/BioC error or challenge responses are not treated as primary full text.
One protein-complex scaffold core represents the organizing work, with postsynaptic-specialization organization and peripheral PSD-membrane location. Membrane recruitment is described within that mechanism. No new biological-process annotation or duplicate nested scaffold activity is proposed. The actual GO-CAM index has no target match. MAPK-scaffold specificity is not adopted merely from Raf binding because its definition requires a multi-kinase cascade assembly.
The accompanying source index provides genuine cache hashes, source URLs, exact record identifiers and selected read ranges. Raw primary responses remain in temporary evidence receipts. It is an authored locator index, not an independent source for its own interpretations; per-row support cites the underlying papers. Short verbatim anchors occur only once in YAML. The aggregate audit covers YAML, these notes and the source index; no long primary passages are embedded here or repeated in the index.
The SAM-pair refinement now uses GO:0032093 SAM domain binding. Actual original PMID:18287031 Results and Methods describe purified human CNK2 5–84 and fly HYP 21–98, domain-specific pull-down controls, SPR, crystallography and interface mutations. The 1:1 heterodimer remains a measured property of the same interaction. The cellular RAF experiments use fly CNK/HYP; a cross-species human-CNK/fly-HYP complex did not recruit fly KSR in the reported assay. No human RAF catalytic or native human HYP-complex claim follows. The protected abstract cache is unchanged; the genuine full normal variant and its selected paragraph locators remain separately identified in the evidence index. PMID:18287031(https://pmc.ncbi.nlm.nih.gov/articles/PMC2268546/)
The earlier uninspected-PAINT statements above describe the initial review boundary and are superseded here. Actual current-main PTHR12844 IBD rows identify the Bilateria PTN000303668 and CNKSR2/Euteleostomi PTN002656117 assertions and their seeds. Genuine PANTHER19 tree and MSA responses were recovered and read at those nodes, the target/donor leaves and selected SAM alignment windows. Human Q8WXI2/PTN002489911 descends through both nodes; its ungapped, case-normalized alignment is exactly the official 1,034-aa sequence. Rat, mouse and human CNKSR2 leaves lie within PTN002656117, whereas human CNKSR1 and fly cnk branch elsewhere below Bilateria. This is actual topology rather than taxonomy alone. It authenticates the current placement/seed role, including rat RGD:708454 on plasma membrane, without pretending to recover the entire historical curator session or changing current donor evidence codes. The GO:0140378 refinement describes the experimentally established CNKSR2-lineage scaffold; it does not relabel the whole ancestral Bilateria assertion. PANTHER tree, alignment
The broad signaling and postsynapse-process ACCEPT actions remain: an existing broader annotation can represent core biology without every ancestor being repeated in the compact core summary. Qualifier wording is not a basis for downgrading them. The membrane refinement explicitly consolidates existing specific coverage and is not NEW. Human Ral/Rlf interactions remain valid abstract-supported biological context, but a new small-GTPase-binding assertion is not manufactured in this finite amendment without resolving its distinct assay/product and coverage scope. The original Raf/EGFR refinements adjudicate pre-existing assertions; that difference does not deny Ral/Rlf association. The afadin interaction contributes to the integrated postsynaptic scaffold account; no additional generic binding row or redundant core is added. The previously inspected original mouse study remains cited. PMID:14597674(https://pubmed.ncbi.nlm.nih.gov/14597674/), PMID:36803960(https://pubmed.ncbi.nlm.nih.gov/36803960/)
A brief disease context is added from the preserved official UniProt DISEASE field (Houge-type X-linked syndromic intellectual developmental disorder). Its underlying clinical papers were not newly inspected for this finite follow-up. The earlier genuine provider timeout/quota failure remains recorded; no provider rerun or fabricated research report was needed for these resolved source-specific issues.