The review preserves all 575 deterministic source annotations from 577 raw GOA records. Three raw records have identical seeded source fields and form one annotation; assignment/date identifiers remain in the source reconciliation. All three official product identities are retained. Normal UniProt, GOA, publication, GO-CAM and provider outputs remain machine-source records.
The biological synthesis is one synaptic receptor adaptor function: receptor recognition, SH3–GK recruitment and postsynaptic structural support cooperate in receptor organization. The source guide records primary-source locators, product/construct distinctions, pathway paths and actual access limits. The public measurement artifact makes every original fragmentomics value and sequence selection reproducible.
Positive binding interfaces are retained without assuming native full-length interactions or deriving physiological peptide-binding function from short assay reagents. Independent APBA1 co-complex and DLGAP4 GK evidence are explicitly separated from their zero-composite PDZ assays. Repeated partners were checked across sources; differences in the targeted phosphorylation assays and the disputed ERBB4 report preserve their particular evidence scopes.
The final calcium-sign refinement follows the original Figure 3 and shRNA Results of PMID:20531396(https://pmc.ncbi.nlm.nih.gov/articles/PMC2927054/): its inhibitory 5-HT2A context does not imply a global calcium effect. The original positive annotation remains unchanged as imported metadata. Positive mouse epithelial junctional localization is retained separately from unresolved DLG4 polarity. The KCl experiments establish regulated degradation, while their process assignment remains over-extended for the specific assay.
PMID:16767099(https://pubmed.ncbi.nlm.nih.gov/16767099/) is flagged DISPUTED because of the verified expression of concern, not marked retracted. This does not negate independent ERBB4 association studies.
The default research-provider attempts failed with authentication/quota responses; no provider report was fabricated. Manual primary-source research and the independent core consultation supply the synthesis. Normal caches retain their actual access flags, including abstracts for papers whose originals were separately recovered or partly indexed. No completion credit is implied by this review record.
The shared PMID:10725395 publication file is an explicit exception to the initial cache set: its genuine full-text DLG3 cache was adopted unchanged after identity and byte reconciliation. The original abstract-only fetch remains preserved in provenance. No flag or publication text was manually edited.
PSD-95 combines receptor-adaptor contacts with a physical contribution to postsynaptic-density architecture. Human SH3–GK fragment experiments demonstrate phosphorylation-sensitive partner recognition; rat-neuron immunogold and tomography place PSD-95 in vertical structural elements, and depletion removes patches of PSD material. The two structured core entries describe cooperating molecular roles, not separate proteins or independent catalytic pathways. Rat tomographic receptor assignments are putative, and the structural observations are not claimed as direct human ultrastructure measurements (PMID:22117215(https://pmc.ncbi.nlm.nih.gov/articles/PMC3243629/); PMID:21525273(https://pubmed.ncbi.nlm.nih.gov/21525273/)). This explicit structural entry supersedes the earlier single-entry representation above. AMPA clustering, NMDA-associated signaling and plasticity retain their evidence-specific annotations as consequences of receptor organization and scaffold function; one core per downstream phenotype is unnecessary.
The fragmentomics zero composites require assay-specific interpretation. All three matched PDZ measurements for each of the 138 undecided zero-only pairs use DAPF, with normalized binding intensity below 0.05 and no independently positive matched fluorescence-polarization result. These are unquantified interactions under the tested conditions, not measured zero affinity or biological nonbinding. Negative intensities describe depletion relative to the control/noise. The original study uses different thresholds for other holdup formats and explicitly cautions against a noninteraction inference below threshold; isolated fragments also do not establish a native full-length complex (PMID:36115835(https://pmc.ncbi.nlm.nih.gov/articles/PMC9482650/)).
The calcium-sign refinement remains specific to the 5-HT2A neuronal assay: receptor antagonist, terminal-mutant peptide and scrambled-shRNA controls support an inhibitory PSD-95 context, without a global calcium-regulation claim (PMID:20531396(https://pmc.ncbi.nlm.nih.gov/articles/PMC2927054/), Figure 3). High-KCl experiments instead measure regulated PSD-95 degradation; the significant extra MAP1A effect is on PSD-93. The observed abundance change is retained without claiming that the degraded PSD-95 performs the potassium-response step (PMID:26609151(https://pubmed.ncbi.nlm.nih.gov/26609151/), Results/Figure 7).
The current official GO:0099562 definition says presynaptic despite its postsynaptic label and the explicit part_of edge from structural constituent of postsynaptic density. This ontology-text discrepancy is recorded, not converted into a presynaptic functional assertion. All original annotations, products and machine caches remain unchanged.
Rows: GO:0005783 IEA (GO_REF:0000107, from mouse Q62108) and ISS (GO_REF:0000024, mouse Q62108), both located_in; no ER sub-compartment rows.