This guide accompanies genuine FRMPD4 acquisition through the repository's native tools. All 76 original GOA contexts, all 16 columns of the 76-row export and all 76 genuine native seed objects have been reconciled by exact source key. Actual TSV physical lines and stored indices are recorded separately from the preserved private forecast. Original partners, qualifiers, evidence codes and null extensions remain intact. No new annotations or quotations are proposed.
The main functional evidence uses human FRMPD4 constructs alongside rodent neurons and tissue. The current official sequence is 1322 residues; no alternative-products declaration was found. Experimental fragments, disease truncations and rodent immunoreactive bands are not treated as separate natural human products.
For PMID:36115835, all 53 original partner contexts were joined to the original supplementary measurements and retained curated records. Thirty-one have positive quantitative support and 22 remain unresolved because their matched original signals are below the assay thresholds. A composite zero or the imported kd:1.0x10(molar) value is not interpreted as a physical affinity; negative=false does not establish detectability. No unresolved row is removed or declared biologically absent.
Twenty-seven positive contexts measure the human FRMPD4 C-terminal motif (1313–1322) binding a partner PDZ domain and support a PDZ-domain-binding refinement. Four positive contexts measure FRMPD4’s own PDZ domain (67–160) binding the partner peptide and retain generic binding. TJP3 is the critical reverse-orientation example. LNX1, PARD3B and GRIP2 have useful positive author rows beyond finite-parameter coverage in the exact curated records. Domain-specific missing cells remain missing.
Official UniProt identifies this human brain cDNA sequencing paper as a source of the FRMPD4 sequence. The article was not independently inspected for a FRMPD4 functional assay; sequence identity is not evidence for a neuronal mechanism.
Official citation and sequence provenance only; no selected original functional reading.
Public access: https://pubmed.ncbi.nlm.nih.gov/9205841/, https://doi.org/10.1093/dnares/4.2.141.
Human full-length cDNA sequencing is relevant to the canonical sequence provenance. The authentic cached abstract and UniProt reference positions were checked; no FRMPD4-specific functional experiment was independently read.
Authentic abstract and official UniProt metadata only.
Public access: https://pubmed.ncbi.nlm.nih.gov/14702039/, https://doi.org/10.1038/ng1285.
The Mammalian Gene Collection is a sequence resource cited by the official record. It does not supply the reviewed spine or interaction mechanism in the inspected material.
Authentic cached abstract and official citation metadata; no target-specific original functional assay read.
Public access: https://pubmed.ncbi.nlm.nih.gov/15489334/, https://doi.org/10.1101/gr.2596504.
Selected original Methods and Results establish human FRMPD4 construct interactions, FERM–PIP2 binding and spine-density effects in rat neurons. Rat brain complexes, human transfected protein and purified fragments are distinguished. The WW–F-actin sedimentation result is negative; cellular colocalization is not direct actin binding.
Selected indexed original Methods, Results, Discussion and Figures 1–8 captions; no figure pixels or supplement inspected. Main normal cache is abstract-only.
Public access: https://pubmed.ncbi.nlm.nih.gov/19118189/, https://doi.org/10.1523/JNEUROSCI.3112-08.2008, https://pmc.ncbi.nlm.nih.gov/articles/PMC6671232/, https://www.jneurosci.org/content/jneuro/28/53/14546.full.pdf.
Official UniProt cites identification by mass spectrometry in the T-cell receptor phosphoproteomic study. The authentic abstract was checked, but no exact FRMPD4 peptide or functional result was independently replayed. No kinase or T-cell process is inferred for FRMPD4.
Authentic cached abstract and official reference-position metadata only.
Public access: https://pubmed.ncbi.nlm.nih.gov/19690332/, https://doi.org/10.1126/scisignal.2000007.
Original main text includes direct binding/competition involving FRMPD4 residues 978–1025 and LGN, despite the title foregrounding Inscuteable. The crystal in this paper is mInsc–LGN, not FRMPD4; mInsc cellular/spindle results are not assigned to FRMPD4. Later PMID:25664792 corroborates human fragment identity.
Selected indexed original Results, main Methods, Discussion and Fig. 3 caption. SI cloning details were inaccessible; no image-derived affinity used.
Public access: https://pubmed.ncbi.nlm.nih.gov/22074847/, https://doi.org/10.1073/pnas.1110951108, https://pmc.ncbi.nlm.nih.gov/articles/PMC3228485/, https://www.researchgate.net/publication/51790695_Structural_basis_for_interaction_between_the_conserved_cell_polarity_proteins_Inscuteable_and_Leu-Gly-Asn_repeat-enriched_protein_LGN.
Selected original construct text explicitly uses full-length rat Preso1 from a rat-brain cDNA library. Rat/mouse binding, knockout and rescue experiments support an anchoring mechanism involving Homer, mGluR and proline-directed kinases; FRMPD4 is not the kinase. This is conserved mechanistic context, not a human-clone assay merely because HEK293T was used.
Selected indexed original Methods/Results/captions and construct excerpts. Direct EuropePMC XML returned a preserved 16-byte HTTP 500 response; no claim of recovered full XML, complete paper, images or supplements.
Public access: https://pubmed.ncbi.nlm.nih.gov/22561452/, https://doi.org/10.1038/nn.3103, https://pmc.ncbi.nlm.nih.gov/articles/PMC3434267/.
Original SI Table S1 explicitly recovers human FRPD4_HUMAN KIKETTV against DLG1 PDZ2 (15/12 replicate counts). Human terminal peptides displayed on phage establish the oriented molecular contact, not a full-length physiological complex. The original target pair is verified even though the current IntAct target response lacks it.
Selected original main Methods plus actual original SI PDF Methods and Table S1 text read. Main cache contains abstract/Discussion; SI figure pixels and other data files not inspected.
Public access: https://pubmed.ncbi.nlm.nih.gov/24550280/, https://doi.org/10.1073/pnas.1312296111, https://pmc.ncbi.nlm.nih.gov/articles/PMC3932933/, https://www.ebi.ac.uk/biostudies/files/S-EPMC3932933/1312296111_pnas.201312296SI.pdf.
The original cached article describes human FRMPD4 variants in intellectual-disability families. Selected FRMPD4 clinical paragraphs were read. Functional knockdown experiments for Clcn4 and Cnksr2 in the same article are not FRMPD4 experiments and are not transferred.
Selected FRMPD4 clinical Results from genuine cached full article; no patient-specific protein abundance or functional rescue assigned.
Public access: https://pubmed.ncbi.nlm.nih.gov/25644381/, https://doi.org/10.1038/mp.2014.193.
The selected original explicitly identifies human FRMPD4 978–1025 and LGN 13–414. Its actual 1.5 Å complex, synthetic peptides, ITC and interface substitutions support direct LGN binding. Fragment structure is separate from cellular complex stoichiometry, natural products and spindle-orientation physiology.
Selected indexed original Methods 2.1/2.4/2.5, Results 3.1 and selected 3.2/Fig. 3 caption; not every paragraph, SI or figure pixels.
Public access: https://pubmed.ncbi.nlm.nih.gov/25664792/, https://doi.org/10.1107/s2053230x14028143, https://pmc.ncbi.nlm.nih.gov/articles/PMC4321472/.
Original human clinical and transfected-construct evidence connects FRMPD4 disruption to X-linked intellectual disability and altered scaffold interactions. Human WT versus p.Cys618Valfs*8 co-IP with Homer1c is positive source evidence; the curated mouse Q9Z214-1 partner remains exact. Overexpression of a predicted truncation is not proof of its endogenous abundance in patients.
Selected indexed author-paper main Methods/Results/Discussion and captions. No complete-paper/SI/image claim; selected neuronal-culture paragraph does not itself establish species.
Public access: https://pubmed.ncbi.nlm.nih.gov/29267967/, https://doi.org/10.1093/hmg/ddx426, https://pmc.ncbi.nlm.nih.gov/articles/PMC5886117/, https://www.researchgate.net/publication/322008400_FRMPD4_mutations_cause_X-linked_intellectual_disability_and_disrupt_dendritic_spine_morphogenesis.
Human WT FRMPD4 terminal peptide is selected by partner PDZ domains. Actual Table EV3 verifies DLG1/SCRIB rows; original Fig. 5A pixels verify positive WT LPKIKETTV bars for SNTB1, SNTA1, DLG4 PDZ3 and DLG3 PDZ2, without extracting numeric values. T1320E is a phosphomimetic library comparison; no endogenous FRMPD4 phosphosite or kinase claim follows.
Genuine original XML selected Methods/Results/captions; actual Table EV3 target cells and original Fig. 5A image read. EV8/9 were inspected but do not establish residue-specific phosphorylation chemistry for FRMPD4.
Public access: https://pubmed.ncbi.nlm.nih.gov/30126976/, https://doi.org/10.15252/msb.20178129, https://pmc.ncbi.nlm.nih.gov/articles/PMC6100724/, https://www.ebi.ac.uk/biostudies/studies/S-EPMC6100724.
The original Table 1 contains the exact MERS E–FRMPD4 PDZ result, despite the SARS-CoV-2 title. Its BI 0.31 / Kd 43 µM supports in-vitro binding to the MERS peptide. Separate viral constructs and knockdown infection endpoints are not assigned to this interaction or used to create an infection-process annotation.
Selected indexed original Methods, Results and Table 1/2 text; direct XML failed. No figure pixels or supplementary raw measurements inspected.
Public access: https://pubmed.ncbi.nlm.nih.gov/33864728/, https://doi.org/10.1111/febs.15881, https://pmc.ncbi.nlm.nih.gov/articles/PMC8250131/, https://orbi.uliege.be/bitstream/2268/265221/1/febs.15881.pdf.
The original domain–motif affinity study is relevant, but the quantitative source audit is essential: 31 of 53 original partner contexts have matched positive measurements, whereas 22 have only below-threshold original signals/composite zero and an unresolved 10-M-looking curated parameter. negative=false alone is insufficient. Twenty-seven positive contexts have the FRMPD4 terminal peptide binding partner PDZ domains; four support only the reverse orientation. The original source remains valid while these specific imported assertions stay unresolved.
Genuine original XML selected Methods, actual original Supplementary Dataset 1 cells/legend, all 53 partner joins and numeric matches independently replayed. Both human fragments 67–160 and 1313–1322 are distinguished. No in-vivo/full-length affinity inference.
Public access: https://pubmed.ncbi.nlm.nih.gov/36115835/, https://doi.org/10.1038/s41467-022-33018-0.
The genuine dated PANTHER 19 tree, MSA, family FASTA and AN/PTN mapping identify human Q14CM0 as AN143/PTN002551300, with its full 1322-residue sequence matching the official record. Both incoming IBDs are placed at AN135/PTN008705583. Their human self-donor is experimentally grounded in PMID:19118189 and is valid descendant evidence. The two terms are PIP2 binding and dendritic spine; the latter preserves the original is_active_in relation.
The family contains an off-target gar FASTA/MSA one-residue discrepancy and an extra chimpanzee FASTA record absent from the tree. These are retained in the private source ledger; neither changes the exact human sequence or target ancestry. The dated 188-node tree/MSA remains distinct from the genuine native PAINT slice, which resolves 191 nodes and contains 11 annotation rows. Both original target IBD assertions match exactly; other native rows are retained without inferring additional target functions.
Official is_a ancestry confirms PDZ domain binding under protein binding and dendritic spine under postsynapse. The postsynapse row is therefore too general relative to the retained spine annotations. Generic positive associations whose demonstrated orientation or function does not justify a specific refinement remain non-core.
The 17 normal sources have now been acquired or reused: 11 existing main files remain byte-identical, while six absent paths were filled through native tooling after qualification. Both existing PANTHER family files were materialized before unforced gene fetching. PMID:22561452 was fetched as the selected auxiliary; the UniProt-only references PMID:25664792 and PMID:9205841 required explicit native fetches because gene fetching acquired the GOA references only. The untouched genuine PENDING seed is archived, and all source files remain unchanged. The reviewed canonical annotations retain every original machine field and the genuine stored order. Provider credential holds remain in effect; no provider retry or provider-labelled output was produced.
Cache availability flags describe the acquired files and do not establish that every original method, image or supplement was inspected. The selected original reading limits in each entry above remain authoritative.
| PMID | Current cache reports full text | Acquisition |
|---|---|---|
| PMID:14702039 | no | reused exact main bytes |
| PMID:15489334 | no | reused exact main bytes |
| PMID:19118189 | no | reused exact main bytes |
| PMID:19690332 | no | reused exact main bytes |
| PMID:22074847 | yes | native acquisition |
| PMID:22561452 | yes | native acquisition |
| PMID:24550280 | yes | reused exact main bytes |
| PMID:25644381 | yes | reused exact main bytes |
| PMID:25664792 | yes | native acquisition |
| PMID:29267967 | yes | native acquisition |
| PMID:30126976 | no | reused exact main bytes |
| PMID:33864728 | no | reused exact main bytes |
| PMID:36115835 | yes | reused exact main bytes |
| PMID:9205841 | no | native acquisition |
The quantitative fragment audit provides a standard-library replay from the original PMID:36115835 workbook, a checksum-pinned source URL, the 189 exact matched curated records and all 713 target measurement rows. Its 53-context summary distinguishes 31 positive original fragment measurements from 22 unresolved imported assertions. Each matched row exposes its measured BI and method-specific cutoff; the optional affinity-sensitivity calculation is explicitly labeled as derived under the usual 4 µM PDZ assumption, not an author-reported threshold. The source evidence archive preserves machine provenance and reviews; the audit supplies independent measurements rather than another copy of the biological synthesis.
For PMID:19118189, the accessible original article has the Methods heading F-actin cosedimentation assay and Results heading Preso associates with PIP2 and actin filaments. Figure 3I and its Results explanation report the negative purified-protein sedimentation result with the positive α-actinin control; Figures 3B–H describe positive cellular actin colocalization. These selected text and caption results distinguish indirect association from direct actin binding. No new inspection of the Figure 3 image or supplementary figures is claimed. The same original article's βPix interaction results identify the R102A perturbation of the target's own PDZ module; that module remains distinct from its C-terminal motif binding other proteins' PDZ domains.
The official GO:0030911 definition and is_a ancestry support the TPR-domain-binding refinement of the original PMID:22074847 GPSM2/LGN row, with the independently read human structure/interface assays in PMID:25664792. The original source and partner remain unchanged. The official is_a-only ancestry for GO:0043197 includes GO:0098794 postsynapse, preserving the existing typed broadness rationale.
PMIDs 9205841, 14702039, 15489334 and 19690332 retain their bibliographic and sequence/proteomics provenance, but their reference correctness is UNVERIFIED for target-specific supporting relevance because the relevant original experimental material was not independently established. This does not assert that the identifiers or papers are wrong.