DLG4

Summary: PSD-95 can restrain beta-1-adrenergic receptor internalization.

Reason: The literal rat P31016 donor has experimental grounding in PMID:11526121. Its abstract explicitly contrasts PSD-95-mediated inhibition with MAGI-2-mediated enhancement of receptor internalization. Retain this receptor-specific regulatory context without making inhibition of all receptor internalization the primary DLG4 function; full original construct details were not recovered.

Summary: Specify recognition of the potassium-channel partner.

Reason: The source partner is rat Kcna4 P15385, a transmembrane potassium transporter. The PMID:10433268 abstract establishes the PSD-95/GKAP/Shank assembly but does not expose this exact Kcna4 panel. Independent curated PMID:7477295 two-hybrid/far-western records resolve the same human-DLG4/rat-Kcna4 pair and its tail-dependent interface. The refinement denotes transporter binding, not ion transport by DLG4 or the channel activity of a peptide reagent.

Proposed replacements: transmembrane transporter binding

Summary: Specify the GKAP scaffold interaction.

Reason: The literal P97836-5 partner is rat Dlgap1/GKAP isoform 3 (GKAP A), not an unspecified natural DLG4 isoform. The source abstract describes the PSD-95/GKAP/Shank ternary assembly and rat-brain coprecipitation; independent domain studies establish the GKAP interface. Scaffold-protein binding captures the partner role without claiming that coimmunoprecipitation alone measures a purified binary affinity.

Proposed replacements: scaffold protein binding

Summary: Specify binding to the receptor tyrosine kinase ERBB4.

Reason: The original uses a human ERBB4 tail and human-brain two-hybrid library, reciprocal rat-forebrain coimmunoprecipitation, and QT-6 cells expressing human ERBB4 with a C-terminal deletion control. PSD-95 PDZ1/2 recognize the receptor tail. These complementary assays support receptor-tyrosine-kinase binding; the full PSD-95 expression-backbone species is not explicitly resolved, and neither receptor activation nor DLG4 kinase activity is inferred from binding.

Proposed replacements: receptor tyrosine kinase binding

Summary: Specify the kinesin partner class.

Reason: Although the paper foregrounds hDlg/DLG1 in T lymphocytes, its complete abstract explicitly reports GAKIN binding to the PSD-95 guanylate-kinase-like domain and a negative p55 comparison. GAKIN is KIF13B, a kinesin. The controlled qualitative association supports kinesin binding; neither stoichiometric affinity nor a DLG4 transport assay is claimed, and the exact full-paper constructs remain inaccessible.

Proposed replacements: kinesin binding

Summary: Specify potassium-channel tail recognition.

Reason: The target-resolved curated records describe direct fluorescence-polarization and peptide-ELISA interactions between DLG4 PDZ1 and the cytoplasmic tail of a human voltage-gated potassium channel. These assays identify the interface of an established transporter partner; they do not establish DLG4 ion transport, native channel stoichiometry or all-product equivalence. The normal source is abstract-only, so the exact read scope is the abstract plus literal assay/construct records.

Proposed replacements: transmembrane transporter binding

Summary: Specify the established ionotropic glutamate-receptor interface.

Reason: The source-specific curated assays test DLG4 PDZ domains with cytoplasmic NMDA-receptor tail peptides. These are receptor-derived interface measurements within the independently established PSD-95 receptor-adaptor mechanism, not evidence for a free-peptide biological function or a full-length affinity measurement. Preserve the literal receptor/isoform identifier and variant controls; the normal source remains abstract-only.

Proposed replacements: ionotropic glutamate receptor binding

Summary: Specify potassium-channel tail recognition.

Reason: The target-resolved curated records describe direct fluorescence-polarization and peptide-ELISA interactions between DLG4 PDZ1 and the cytoplasmic tail of a human voltage-gated potassium channel. These assays identify the interface of an established transporter partner; they do not establish DLG4 ion transport, native channel stoichiometry or all-product equivalence. The normal source is abstract-only, so the exact read scope is the abstract plus literal assay/construct records.

Proposed replacements: transmembrane transporter binding

Summary: Specify the established ionotropic glutamate-receptor interface.

Reason: The source-specific curated assays test DLG4 PDZ domains with cytoplasmic NMDA-receptor tail peptides. These are receptor-derived interface measurements within the independently established PSD-95 receptor-adaptor mechanism, not evidence for a free-peptide biological function or a full-length affinity measurement. Preserve the literal receptor/isoform identifier and variant controls; the normal source remains abstract-only.

Proposed replacements: ionotropic glutamate receptor binding

Summary: Specify the established ionotropic glutamate-receptor interface.

Reason: The source-specific curated assays test DLG4 PDZ domains with cytoplasmic NMDA-receptor tail peptides. These are receptor-derived interface measurements within the independently established PSD-95 receptor-adaptor mechanism, not evidence for a free-peptide biological function or a full-length affinity measurement. Preserve the literal receptor/isoform identifier and variant controls; the normal source remains abstract-only.

Proposed replacements: ionotropic glutamate receptor binding

Summary: Specify the established ionotropic glutamate-receptor interface.

Reason: The source-specific curated assays test DLG4 PDZ domains with cytoplasmic NMDA-receptor tail peptides. These are receptor-derived interface measurements within the independently established PSD-95 receptor-adaptor mechanism, not evidence for a free-peptide biological function or a full-length affinity measurement. Preserve the literal receptor/isoform identifier and variant controls; the normal source remains abstract-only.

Proposed replacements: ionotropic glutamate receptor binding

Summary: Retain CRIPT-tail recognition as a supporting interaction.

Reason: The literal records measure DLG4 PDZ1/PDZ3 binding to human CRIPT residues 91–101 by fluorescence polarization and peptide ELISA. The positive interface is credible and independently corroborated, but these assays do not establish DLG4 microtubule binding, CRIPT-mediated cytoskeletal remodeling or a separate peptide-binding core. Retain the source assertion with its fragment scope.

Summary: Specify binding to the KIF1Balpha kinesin partner.

Reason: The literal partner O60333-3 is the official KIF1Balpha product, whose reconstructed C terminus retains AGRETTV. The original uses a rat KIF1Balpha tail, GST and two-hybrid assays, terminal-valine mutation and rat-brain association. The imported human pair mapping and original rat construct are kept distinct. Controlled tail recognition supports kinesin binding, without a measured native stoichiometry or a claim that DLG4 itself transports cargo.

Proposed replacements: kinesin binding

Summary: Retain the nonneuronal megalin association.

Reason: The source and literal records identify LRP2/megalin cytoplasmic-tail recognition by PSD-95, with two-hybrid and overexpression coimmunoprecipitation evidence plus colocalization. Megalin is principally an endocytic receptor in this context; the assay does not establish a DLG4-specific signaling-receptor mechanism or transport activity. Preserve the positive association and nonneuronal context without forcing an unsupported functional subclass.

Summary: Retain ERBB4 association with an explicit disputed-source qualification.

Reason: This human postmortem coimmunoprecipitation source has a verified editorial expression of concern (PMID:38114668), citing blot artifacts and possible duplicated bands; it has not been treated as a retraction. Independent PMID:10725395 supports the ERBB4/PSD-95 association. Retain the binding observation conservatively while declining to use the disputed disease-dependent signaling magnitude as a core claim.

Summary: Retain the contextual LRP1 complex association.

Reason: The separately recovered original examines human neuronal/astrocytic cultures in an HIV-Tat-associated LRP1/NMDAR complex context. Coimmunoprecipitation supports membership or association but does not isolate a purified PSD-95–LRP1 binary interface. Retain the positive source-specific association without converting the complex into a new ligand, enzymatic or disease-specific DLG4 function.

Summary: Specify NMDA-receptor association within the tested complex.

Reason: The source examines the LRP1/PSD-95/NMDAR complex in human neuronal and astrocytic cultures under the reported HIV-Tat context. Its coimmunoprecipitation is complex-level evidence; direct NMDA-receptor tail recognition is independently supported. The receptor-binding refinement uses the combined evidence and does not misdescribe this particular coimmunoprecipitation as a purified binary assay.

Proposed replacements: ionotropic glutamate receptor binding

Summary: Specify recognition of the cytoskeletal regulator Preso.

Reason: The original identifies FRMPD4/Preso as a PSD-95-associated regulator of dendritic-spine actin organization and excitatory transmission, with interaction and domain-control experiments. GO:0005519 denotes binding a protein that modulates cytoskeletal reorganization, which fits Preso. It does not assert that PSD-95 itself catalyzes actin remodeling or that the independently documented SAP102 interaction is the only MAGUK tested.

Proposed replacements: cytoskeletal regulatory protein binding

Summary: Retain the NETO1 association in its cross-species construct context.

Reason: The original uses mouse Neto1 and yeast/heterologous experiments, including an explicitly human PSD-95 GW1 construct and PDZ1–3 in HEK-cell coimmunoprecipitation. The partner is a receptor-associated auxiliary protein; association does not establish that PSD-95 binds glutamate or that Neto1 itself is the NMDA receptor pore. Retain this supporting interaction rather than transfer the function of the whole receptor complex.

Summary: Specify the directly measured NMDA-receptor tail interface.

Reason: Recombinant PSD-95 PDZ1/2 binding to the NR2B tail is a positive fluorescence-polarization assay in this original. Negative results for screened small-molecule inhibitors do not negate the receptor interaction. This supports ionotropic glutamate-receptor binding while retaining the isolated-domain/tail assay scope.

Proposed replacements: ionotropic glutamate receptor binding

Summary: Retain the positive CRIPT–PDZ3 control interaction.

Reason: The original directly uses CRIPT-tail binding to PSD-95 PDZ3 as a positive fluorescence-polarization control. It establishes a selective interface, not a whole-protein neuronal mechanism or general physiological recognition of free peptides. Negative inhibitor screens are not treated as negative CRIPT binding.

Summary: Specify binding to the BCR/ABR GTPase-activating proteins.

Reason: The original tests BCR and ABR motif-dependent PSD-95 interactions with yeast, GST/heterologous assays and rat-brain complexes. Both partners have GTPase-activating roles; this class describes the recognized partners without transferring GAP catalysis to DLG4. The study also shows their spine localization does not require the PSD-95 interaction, so binding is not converted into an obligatory targeting mechanism.

Proposed replacements: GTPase activating protein binding

Summary: Specify recognition of postsynaptic DLGAP scaffolds.

Reason: The literal source tests a PSD-95 guanylate-kinase-like fragment (residues 546–724) against the identified DLGAP partner in the neuronal interaction map. The partner is a postsynaptic scaffold and the class is consistent with independent DLGAP/PSD-95 domain biology. Preserve the positive fragment interaction without claiming that every pair received the paper-wide orthogonal validation or that a full-length affinity was measured.

Proposed replacements: scaffold protein binding

Summary: Specify recognition of the SPAR GTPase-activating protein.

Reason: The map records PSD-95 fragments 298–550 and 546–724 interacting with SIPA1L1/SPAR. SPAR has a Rap GTPase-activating role, and independent targeted human PSD-95 SH3-GK experiments support the interaction. The class concerns the binding partner, not GAP activity of DLG4; high-throughput fragment detection is not relabeled as a native full-length complex assay.

Proposed replacements: GTPase activating protein binding

Summary: Specify alpha-actinin recognition.

Reason: The literal neuronal-map assay links PSD-95 residues 298–550 to ACTN2, an F-actin-crosslinking alpha-actinin. GO:0051393 names that binding partner class without assigning actin binding or bundling to DLG4. The result is a retested fragment interaction, not a claim that this exact pair was among the randomly selected mammalian coimmunoprecipitation validations.

Proposed replacements: alpha-actinin binding

Summary: Specify the established NMDA-receptor partner class.

Reason: The literal human interaction record supports the PSD-95/NMDA-receptor pair in the cited two-hybrid mapping study. Independent receptor-tail assays establish the same class-specific interface. Preserve the exact mapped construct scope and do not equate a two-hybrid positive with a measured full-length membrane complex or an independent ion-channel activity of DLG4.

Proposed replacements: ionotropic glutamate receptor binding

Summary: Retain the fragment-map RALBP1 association.

Reason: The literal neuronal-map record tests PSD-95 residues 298–550 against RALBP1. Although RALBP1 is a multifunctional GAP/scaffold, this fragment-screen result does not resolve which physiological RALBP1 role the DLG4 association serves. Keep the positive binding evidence without automatically importing a GAP, transporter or adaptor subclass from the partner annotation.

Summary: Retain the PRR16 fragment-map interaction.

Reason: The neuronal interaction map contains a positive, retested DLG4–PRR16 association. It does not establish a more specific partner-dependent molecular role for DLG4 or demonstrate that this individual pair underwent every orthogonal assay reported for the study. Preserve positive binding as non-core with the construct limitation.

Summary: Specify recognition of postsynaptic DLGAP scaffolds.

Reason: The literal source tests a PSD-95 guanylate-kinase-like fragment (residues 546–724) against the identified DLGAP partner in the neuronal interaction map. The partner is a postsynaptic scaffold and the class is consistent with independent DLGAP/PSD-95 domain biology. Preserve the positive fragment interaction without claiming that every pair received the paper-wide orthogonal validation or that a full-length affinity was measured.

Proposed replacements: scaffold protein binding

Summary: Specify phosphorylation-dependent recognition by the SH3-GK module.

Reason: The original explicitly uses human PSD-95 SH3-GK residues 426–724 or GK residues 531–724 to recognize phosphorylated DLGAP1, SPAR or LGN-derived ligands. The literal LGN partner is mouse Q8VDU0. These PSD-95 assays are distinct from the SAP97 structural experiments. Phosphoprotein binding captures the measured recognition mechanism; it does not infer kinase activity, all-product equivalence or full-length native stoichiometry.

Proposed replacements: phosphoprotein binding

Summary: Specify phosphorylation-dependent recognition by the SH3-GK module.

Reason: The original explicitly uses human PSD-95 SH3-GK residues 426–724 or GK residues 531–724 to recognize phosphorylated DLGAP1, SPAR or LGN-derived ligands. The literal LGN partner is mouse Q8VDU0. These PSD-95 assays are distinct from the SAP97 structural experiments. Phosphoprotein binding captures the measured recognition mechanism; it does not infer kinase activity, all-product equivalence or full-length native stoichiometry.

Proposed replacements: phosphoprotein binding

Summary: Specify phosphorylation-dependent recognition by the SH3-GK module.

Reason: The original explicitly uses human PSD-95 SH3-GK residues 426–724 or GK residues 531–724 to recognize phosphorylated DLGAP1, SPAR or LGN-derived ligands. The literal LGN partner is mouse Q8VDU0. These PSD-95 assays are distinct from the SAP97 structural experiments. Phosphoprotein binding captures the measured recognition mechanism; it does not infer kinase activity, all-product equivalence or full-length native stoichiometry.

Proposed replacements: phosphoprotein binding

Summary: Specify binding to the E3 ubiquitin ligase MDM2.

Reason: The original includes PSD-95/MDM2 coimmunoprecipitation and recombinant GST/His interaction assays in the source-specific mouse/heterologous context. MDM2 is the E3 enzyme; PSD-95 is its binding partner and ubiquitination substrate. GO:0031625 captures that interaction without making DLG4 a ligase or a participant in proteolysis merely because it is degraded.

Proposed replacements: ubiquitin protein ligase binding

Summary: Retain motif-dependent association with the orphan receptor GPR85.

Reason: The actual original tests a human GPR85 C-terminal sequence against PSD-95 in mouse-brain and COS-cell extracts. Deleting YCVI abolishes the association and PDZ1 is implicated. This is controlled receptor-tail recognition, but the receptor remains orphan and the assay does not resolve a DLG4-dependent ligand-triggered signaling function. Keep the positive association without inferring a specific signaling subclass or transferring the reported GPR85-variant phenotypes.

Summary: Retain ADAM22 association in the neuronal scaffold.

Reason: The source tests human ADAM22 variants: wild type and C401Y retain PSD-95 binding, whereas the frameshift removing the terminal PDZ-binding motif does not. ADAM22 is a noncatalytic metalloprotease-like receptor. This supports scaffold association without enzyme-binding inference from its family name or a claim that PSD-95 has ADAM22 ligand activity.

Summary: Retain the source-specific PDZ3–tail interaction.

Reason: The literal source records a DLG4 PDZ3 construct (residues 313–388) against a nine-residue partner tail in the phosphomimetic phage-display study. The library compares native and S/T-to-Glu variants; such a display hit is not full-length physiological validation or direct evidence of phosphorylation in cells. Preserve the positive interface without assigning a separate peptide function or automatically transferring the full partner class to DLG4.

Summary: Specify Preso recognition using the independent physiological evidence.

Reason: The source maps DLG4 PDZ3 to the FRMPD4/Preso C-terminal tail, with the phosphomimetic-library scope retained. Independent PMID:19118189 establishes Preso as a PSD-95-associated cytoskeletal regulator. GO:0005519 therefore has biological support beyond the peptide-display reagent; no full-length validation is claimed for the display experiment itself.

Proposed replacements: cytoskeletal regulatory protein binding

Summary: Retain the source-specific PDZ3–tail interaction.

Reason: The literal source records a DLG4 PDZ3 construct (residues 313–388) against a nine-residue partner tail in the phosphomimetic phage-display study. The library compares native and S/T-to-Glu variants; such a display hit is not full-length physiological validation or direct evidence of phosphorylation in cells. Preserve the positive interface without assigning a separate peptide function or automatically transferring the full partner class to DLG4.

Summary: Retain the source-specific PDZ3–tail interaction.

Reason: The literal source records a DLG4 PDZ3 construct (residues 313–388) against a nine-residue partner tail in the phosphomimetic phage-display study. The library compares native and S/T-to-Glu variants; such a display hit is not full-length physiological validation or direct evidence of phosphorylation in cells. Preserve the positive interface without assigning a separate peptide function or automatically transferring the full partner class to DLG4.

Summary: Retain the source-specific PDZ3–tail interaction.

Reason: The literal source records a DLG4 PDZ3 construct (residues 313–388) against a nine-residue partner tail in the phosphomimetic phage-display study. The library compares native and S/T-to-Glu variants; such a display hit is not full-length physiological validation or direct evidence of phosphorylation in cells. Preserve the positive interface without assigning a separate peptide function or automatically transferring the full partner class to DLG4.

Summary: Retain the source-specific PDZ3–tail interaction.

Reason: The literal source records a DLG4 PDZ3 construct (residues 313–388) against a nine-residue partner tail in the phosphomimetic phage-display study. The library compares native and S/T-to-Glu variants; such a display hit is not full-length physiological validation or direct evidence of phosphorylation in cells. Preserve the positive interface without assigning a separate peptide function or automatically transferring the full partner class to DLG4.

Summary: Retain the source-specific PDZ3–tail interaction.

Reason: The literal source records a DLG4 PDZ3 construct (residues 313–388) against a nine-residue partner tail in the phosphomimetic phage-display study. The library compares native and S/T-to-Glu variants; such a display hit is not full-length physiological validation or direct evidence of phosphorylation in cells. Preserve the positive interface without assigning a separate peptide function or automatically transferring the full partner class to DLG4.

Summary: Retain the source-specific PDZ3–tail interaction.

Reason: The literal source records a DLG4 PDZ3 construct (residues 313–388) against a nine-residue partner tail in the phosphomimetic phage-display study. The library compares native and S/T-to-Glu variants; such a display hit is not full-length physiological validation or direct evidence of phosphorylation in cells. Preserve the positive interface without assigning a separate peptide function or automatically transferring the full partner class to DLG4.

Summary: Retain the APBA1 co-complex association.

Reason: The exact BioPlex record is human APBA1–DLG4 anti-tag coimmunoprecipitation, with the tandem C-terminal tag on APBA1. This is positive co-complex association, not necessarily direct binary binding. The separate zero composite for APBA1 tail/domain measurements does not refute this whole-cell association, and no extra adaptor subclass is inferred from it.

Summary: Retain the TIAM1 fragment interaction.

Reason: The human-brain interaction-map record identifies DLG4 residues 131–306 with TIAM1. The paper-specific DSCAM control fragment is a different construct and is not substituted for the DLG4 record. Retain the positive fragment association without assuming a native neuronal complex or importing a GEF-regulatory role merely from the TIAM1 partner identity.

Summary: Specify the established NMDA-receptor partner class.

Reason: The literal human interaction record supports the PSD-95/NMDA-receptor pair in the cited two-hybrid mapping study. Independent receptor-tail assays establish the same class-specific interface. Preserve the exact mapped construct scope and do not equate a two-hybrid positive with a measured full-length membrane complex or an independent ion-channel activity of DLG4.

Proposed replacements: ionotropic glutamate receptor binding

Summary: Retain the TTC24 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for A2A3L6 (TTC24; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.71313467, PDZ2=4.95032285, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the E6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for A4U7F2 (E6; taxon 37120); maximum source COMP values by tested domain are PDZ1=4.57731572, PDZ2=4.95559468, PDZ3=4.22878709. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SMCHD1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for A6NHR9 (SMCHD1; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.81503968, PDZ2=4.15087457, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SLC15A5 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for A6NIM6 (SLC15A5; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.29042338, PDZ2=4.22215443, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the NCBP2L association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for A6PVI3 (NCBP2L; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.24621548, PDZ2=4.63914613, PDZ3=4.166638. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the KCNJ18 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for B7U540 (KCNJ18; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.66202413, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The PPP1R3G source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for B7ZBB8 (PPP1R3G; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.012306 to 0.021925), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the TMEM178B association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for H3BS89 (TMEM178B; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=3.495263. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the CCL24 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O00175 (CCL24; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.63562141, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ARVCF association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O00192 (ARVCF; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.2, PDZ2=4.81, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SLC1A7 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O00341 (SLC1A7; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.43946332, PDZ2=4.66763364, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the CCRL2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O00421 (CCRL2; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.70574057, PDZ2=4.66355474, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the DLL1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O00548 (DLL1; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.93, PDZ2=4.39, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The CACNA1A source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O00555 (CACNA1A; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.14765 to 0.0034204), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The PODXL source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O00592 (PODXL; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.020234 to -0.0036475), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the CES2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O00748 (CES2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=4.00291642, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the CLDN4 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O14493 (CLDN4; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.53676732, PDZ2=0, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the CIT association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O14578 (CIT; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=3.61997396. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The NHERF1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O14745 (NHERF1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.02236 to -0.00665), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the RGS12 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O14924 (RGS12; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.22, PDZ2=4.13, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The TECPR2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O15040 (TECPR2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.10774 to 0.011311), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The AXIN1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O15169 (AXIN1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.034748 to 0.0025692), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the SLC16A3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O15427 (SLC16A3; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.90339086, PDZ2=4.20358255, PDZ3=3.93946331. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ABCC4 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O15439 (ABCC4; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.22572465, PDZ2=4.22906153, PDZ3=3.85283303. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the CLDN3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O15551 (CLDN3; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.63037365, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the PLXNB1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O43157 (PLXNB1; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.6823779, PDZ2=4.20282772, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ARHGAP6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O43182 (ARHGAP6; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.13175304, PDZ2=4.42062894, PDZ3=3.46083268. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The GRID2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O43424 (GRID2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.061566 to 0.040882), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The AKAP10 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O43572 (AKAP10; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.059764 to 0.011674), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The PRKN source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O60260 (PRKN; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range 0.0057621 to 0.045725), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the EVI5 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O60447 (EVI5; taxon 9606); maximum source COMP values by tested domain are PDZ1=5.78883695, PDZ2=5.8671601, PDZ3=4.44292385. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SLC16A7 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O60669 (SLC16A7; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=4.11227095, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The LPXN source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O60711 (LPXN; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range 0.0033358 to 0.021005), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The CYTIP source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O60759 (CYTIP; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.02788 to 0.00583), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the RAMP3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O60896 (RAMP3; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.0164687, PDZ2=3.97843429, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The NOS1AP source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O75052 (NOS1AP; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.096993 to 0.037344), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The SDC3 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O75056 (SDC3; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.11179 to -0.004912), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the FZD7 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O75084 (FZD7; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.39709875, PDZ2=4.68940004, PDZ3=4.01950325. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the LRP4 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O75096 (LRP4; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.16588307, PDZ2=4.68789973, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The BANF1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O75531 (BANF1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.092659 to 0.0305), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the STK16 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O75716 (STK16; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.87278647, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SLC22A3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O75751 (SLC22A3; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.54934176, PDZ2=0, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the CIB2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O75838 (CIB2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=3.49941559. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the DGKI association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O75912 (DGKI; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.61441891, PDZ2=4.97147496, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the FCHSD2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O94868 (FCHSD2; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.88883909, PDZ2=4.20165093, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SLCO2B1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O94956 (SLCO2B1; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.82831603, PDZ2=3.91485286, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The SBF1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O95248 (SBF1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.047985 to 0.029254), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the ABCC6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O95255 (ABCC6; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.54875336, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The CLDN7 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O95471 (CLDN7; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range 0.03118 to 0.046386), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the ABCA1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O95477 (ABCA1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.52, PDZ2=5.25, PDZ3=3.78. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The CLDN9 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O95484 (CLDN9; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.053869 to 0.048811), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The CLDN14 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O95500 (CLDN14; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.017297 to 0.031125), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the SEMA4F association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O95754 (SEMA4F; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.67129187, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the CLDN1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for O95832 (CLDN1; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.59968389, PDZ2=0, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the TGFA association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P01135 (TGFA; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.75113375, PDZ2=4.82430874, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the E6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 6 sequence-supported measurement(s) for P03126 (E6; taxon 333760); maximum source COMP values by tested domain are PDZ1=4.72821247, PDZ2=4.66473498, PDZ3=5.06144244. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the Tax association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P03409 (Tax; taxon 11926); maximum source COMP values by tested domain are PDZ1=5.21794545, PDZ2=5.51048738, PDZ3=5.33663621. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the MAS1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P04201 (MAS1; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.97996409, PDZ2=4.45452983, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ERBB2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P04626 (ERBB2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.47558014, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the GYPC association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P04921 (GYPC; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.60703067, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the E6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P06427 (E6; taxon 10586); maximum source COMP values by tested domain are PDZ1=4.57001477, PDZ2=4.77198838, PDZ3=5.32016033. The selected nonzero composite supports the isolated PDZ–ligand interface. The three unmatched HPV33-E6 phosphopeptide candidates are excluded from the selected mapping; the positive interpretation uses sequence-supported measurements. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the E6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 6 sequence-supported measurement(s) for P06463 (E6; taxon 333761); maximum source COMP values by tested domain are PDZ1=5.10527909, PDZ2=5.46125705, PDZ3=5.73528449. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The ADRB2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P07550 (ADRB2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range 0.0129 to 0.03303), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the IGF1R association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P08069 (IGF1R; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.76483572, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the PFKM association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P08237 (PFKM; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.93283903, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ADRB1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P08588 (ADRB1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.03432495, PDZ2=4.22260487, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the TMEM225B association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P0DP42 (TMEM225B; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.59615495, PDZ2=4.049807, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The POLR1D source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P0DPB6 (POLR1D; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.055257 to 0.044521), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The E source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P0DTC4 (E; taxon 2697049); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.0025863 to 0.017853), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The KIT source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P10721 (KIT; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.011862 to 0.016607), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the HSPA5 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P11021 (HSPA5; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.50289662, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SLC2A1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P11166 (SLC2A1; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.50757116, PDZ2=3.94960459, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SLC2A3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P11169 (SLC2A3; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.12245866, PDZ2=4.21291421, PDZ3=3.69631721. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Specify the independently supported BCR partner class.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P11274 (BCR; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.67191575, PDZ2=4.8124892, PDZ3=3.69592016. Independent BCR/ABR motif-controlled cellular and brain assays establish the GTPase-activating partner context. This does not give DLG4 GAP activity. The PDZ-domain/reagent measurements do not establish a native full-length complex, endogenous affinity or equivalent behavior of all DLG4 products.

Proposed replacements: GTPase activating protein binding

Summary: The SRC source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P12931 (SRC; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.010196 to 0.048364), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The CFTR source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P13569 (CFTR; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.0058475 to 0.012191), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the NCF1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P14598 (NCF1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=4.51025812, PDZ3=3.66833886. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The JUP source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P14923 (JUP; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.11481 to 0.005817), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the CD46 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P15529 (CD46; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.69782878, PDZ3=4.30413982. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The ATP2A2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P16615-3 (ATP2A2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.14914 to 0.019254), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the PRKCA association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P17252 (PRKCA; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.07099146, PDZ2=4.53253206, PDZ3=3.87534123. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The GJA1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P17302 (GJA1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.020955 to 0.018277), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the E6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P17386 (E6; taxon 10585); maximum source COMP values by tested domain are PDZ1=5.0249168, PDZ2=5.35902182, PDZ3=5.09869107. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The PRKACA source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P17612 (PRKACA; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.10687 to 0.0097164), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the TYRP1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P17643 (TYRP1; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.90572965, PDZ2=4.10833643, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ATP2B1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P20020 (ATP2B1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.06281728, PDZ2=4.14506443, PDZ3=4.00628512. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The NEB source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P20929 (NEB; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.085583 to -0.0089703), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Specify the independently supported KCNA4 partner class.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P22459 (KCNA4; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.66579999, PDZ2=5.19232449, PDZ3=0. Independent target-resolved KCNA4 tail assays establish a potassium-transporter interface. DLG4 is not itself a potassium channel. The PDZ-domain/reagent measurements do not establish a native full-length complex, endogenous affinity or equivalent behavior of all DLG4 products.

Proposed replacements: transmembrane transporter binding

Summary: Retain the KCNA5 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P22460 (KCNA5; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.83687197, PDZ2=4.43378082, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The UQCRC2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P22695 (UQCRC2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.084672 to 0.025273), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the PTPRG association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P23470 (PTPRG; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.59015532, PDZ2=5.01415076, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the PTPRZ1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P23471 (PTPRZ1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.65445793, PDZ2=5.09003229, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the MCC association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P23508 (MCC; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.83384861, PDZ3=3.94853477. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ATP2B4 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P23634 (ATP2B4; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.77671475, PDZ2=5.17842314, PDZ3=4.64869516. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The CXCR1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P25024 (CXCR1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.10245 to 0.015896), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the APC association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P25054 (APC; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.38, PDZ2=4.98, PDZ3=4.5. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ADRA1D association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P25100 (ADRA1D; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.88859811, PDZ2=4.54495654, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The CTNNA2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P26232 (CTNNA2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.089519 to 0.017868), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the U2AF2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P26368 (U2AF2; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.61604701, PDZ2=0, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the E6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P26554 (E6; taxon 10595); maximum source COMP values by tested domain are PDZ1=4.89663073, PDZ2=4.99166488, PDZ3=4.75116585. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ACVR2A association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P27037 (ACVR2A; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.32538268, PDZ3=3.70886832. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the E6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P27228 (E6; taxon 10587); maximum source COMP values by tested domain are PDZ1=5.09080267, PDZ2=5.50663889, PDZ3=5.19609602. The selected nonzero composite supports the isolated PDZ–ligand interface. The unmatched HPV35-E6 phosphopeptide candidate with a nonzero composite is excluded. Independently sequence-supported measurements remain positive, so the conclusion does not rely on that identity mismatch. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the HTR2A association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P28223 (HTR2A; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.69172586, PDZ2=4.74163993, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the HTR2C association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P28335 (HTR2C; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.94106256, PDZ2=4.63586792, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The SDC4 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P31431 (SDC4; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.084339 to 0.023143), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the GUCY1A2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P33402 (GUCY1A2; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.02613472, PDZ2=4.49952514, PDZ3=4.86427089. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the MCM7 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P33993 (MCM7; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.76490952, PDZ2=5.11706385, PDZ3=4.33126241. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The SDC2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P34741 (SDC2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.050506 to 0.034741), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the CRHR1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P34998 (CRHR1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.55629176, PDZ2=4.9250185, PDZ3=4.43078855. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The CTNNA1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P35221 (CTNNA1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.09218 to -0.013873), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The CTNNB1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P35222 (CTNNB1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.039353 to 0.025787), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The SSTR5 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P35346 (SSTR5; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.10738 to 0.012355), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the SCN4A association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P35499 (SCN4A; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.97778826, PDZ2=5.7112339, PDZ3=4.38826616. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Specify the independently supported ACTN2 partner class.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P35609 (ACTN2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.60771572, PDZ3=0. The independent neuronal fragment map records the ACTN2 interaction, and the partner is an alpha-actinin crosslinker. The refinement concerns the recognized partner, not actin-crosslinking by DLG4. The PDZ-domain/reagent measurements do not establish a native full-length complex, endogenous affinity or equivalent behavior of all DLG4 products.

Proposed replacements: alpha-actinin binding

Summary: Retain the GJC1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P36383 (GJC1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.50773595, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the MAP2K2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P36507 (MAP2K2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=4.11529486, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the L2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P36762 (L2; taxon 10616); maximum source COMP values by tested domain are PDZ1=3.62, PDZ2=0, PDZ3=4.26. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the E6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P36809 (E6; taxon 10611); maximum source COMP values by tested domain are PDZ1=4.92276181, PDZ2=5.44554092, PDZ3=4.35149536. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SLC26A3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P40879 (SLC26A3; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.66097571, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The GRM5 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P41594 (GRM5; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.079183 to 0.003448), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the GRIA2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P42262 (GRIA2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.73072066, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The GRIA3 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P42263 (GRIA3; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.039443 to 0.025226), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the SLC1A3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P43003 (SLC1A3; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.48893477, PDZ2=0, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The SLC1A1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P43005 (SLC1A1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.084367 to 0.015682), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the SLC1A4 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P43007 (SLC1A4; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.78601479, PDZ2=3.91318894, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The PTGIR source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P43119 (PTGIR; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.099655 to 0.0012969), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The GRK6 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P43250 (GRK6; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.096984 to 0.042701), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the GPR6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P46095 (GPR6; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.74560959, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The SLCO1A2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P46721 (SLCO1A2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.055248 to 0.036508), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The YAP1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P46937 (YAP1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range 0.015434 to 0.038008), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the GPR12 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P47775 (GPR12; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.9221589, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The MTNR1A source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P48039 (MTNR1A; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.11001 to 0.01618), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the KCNJ1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P48048 (KCNJ1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.59374066, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the KCNJ4 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P48050 (KCNJ4; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=4.17034321, PDZ3=4.11944846. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The SLC9A3 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P48764 (SLC9A3; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.073914 to 0.0087458), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The ADGRE5 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P48960 (ADGRE5; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.063332 to 0.014258), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the PTH2R association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P49190 (PTH2R; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.50773834, PDZ2=0, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The PRLHR source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P49683 (PRLHR; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.086497 to 0.0081248), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the GNG4 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P50150 (GNG4; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.05795778, PDZ2=3.95464689, PDZ3=4.16759521. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The PDLIM4 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P50479-1 (PDLIM4; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.041629 to 0.04683), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The PDLIM4 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P50479-2 (PDLIM4; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.04073 to -0.03136), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The RAB9A source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P51151 (RAB9A; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.071916 to 0.032651), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The EFNB2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P52799 (EFNB2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.035999 to 0.028306), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the MAPK12 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P53778 (MAPK12; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=4.4470796, PDZ3=4.03024491. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SLC16A1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P53985 (SLC16A1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.49641771, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the EPHB3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P54753 (EPHB3; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.66444252, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the CLDN8 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P56748 (CLDN8; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.79068616, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The CLDN20 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P56880 (CLDN20; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.04726 to 0.010273), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The JAM2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P57087 (JAM2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.065122 to 0.045071), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the PTEN association with its measured fragment scope.

Reason: The published SD1 workbook resolves 6 sequence-supported measurement(s) for P60484 (PTEN; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.98232436, PDZ2=4.57892578, PDZ3=3.5582274. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The DCAF7 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P61962 (DCAF7; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.039062 to 0.0063689), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The HNRNPK source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P61978-2 (HNRNPK; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.134 to 0.030102), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The TBPL1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P62380 (TBPL1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.022019 to 0.030909), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The TUBB4B source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P68371 (TUBB4B; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.093752 to -0.043245), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the CLDN10 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P78369 (CLDN10; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.52412399, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the JAG1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P78504 (JAG1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.77873992, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ADAM17 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for P78536 (ADAM17; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.32090257, PDZ2=4.34357572, PDZ3=4.42360791. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The PLCB2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q00722 (PLCB2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.029193 to 0.03796), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the CACNA1D association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q01668 (CACNA1D; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=4.02429144, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The SLC6A3 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q01959 (SLC6A3; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range 0.0099859 to 0.039598), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the APBA1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q02410 (APBA1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. Zero composite values do not establish biological noninteraction. Independent BioPlex anti-tag coimmunoprecipitation detects the human APBA1–DLG4 complex. This is positive co-complex evidence despite the unresolved isolated PDZ-tail measurement; it is not proof of a purified direct interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the MUC3A association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q02505 (MUC3A; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=4.16300789, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the GHRHR association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q02643 (GHRHR; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.63241461, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the FKBP4 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q02790 (FKBP4; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.58817805, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The PTH1R source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q03431 (PTH1R; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.0017568 to 0.011724), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Specify the independently supported GRIN1 partner class.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q05586-2 (GRIN1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.1, PDZ2=4.31, PDZ3=0. The exact GRIN1-2 receptor product and corresponding tail are retained. Independent domain assays support the receptor interface; natural GRIN1 products with different tails are not assumed equivalent. The PDZ-domain/reagent measurements do not establish a native full-length complex, endogenous affinity or equivalent behavior of all DLG4 products.

Proposed replacements: ionotropic glutamate receptor binding

Summary: The TYRO3 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q06418 (TYRO3; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.098407 to 0.01187), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the SLC34A1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q06495-1 (SLC34A1; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.51128595, PDZ2=0, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The VAC14 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q08AM6 (VAC14; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.056418 to 0.030069), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Specify the independently supported KCNA1 partner class.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q09470 (KCNA1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.07842764, PDZ2=4.43134245, PDZ3=3.53119908. Independent target-resolved Kv1 channel assays corroborate recognition of the KCNA1 transporter tail, without assigning transport activity to the scaffold. The PDZ-domain/reagent measurements do not establish a native full-length complex, endogenous affinity or equivalent behavior of all DLG4 products.

Proposed replacements: transmembrane transporter binding

Summary: Specify the independently supported GRIN2A partner class.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q12879 (GRIN2A; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.71434773, PDZ2=5.2909802, PDZ3=0. Independent GRIN2A-tail and neuronal interaction-map assays establish the NMDA-receptor interface, beyond the peptide reagent alone. The PDZ-domain/reagent measurements do not establish a native full-length complex, endogenous affinity or equivalent behavior of all DLG4 products.

Proposed replacements: ionotropic glutamate receptor binding

Summary: The TRAF2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q12933 (TRAF2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.020543 to -0.01622), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the FOXI1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q12951 (FOXI1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.47831865, PDZ2=4.62292524, PDZ3=3.57272672. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The GRIK2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q13002 (GRIK2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.048281 to 0.037935), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the TIAM1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q13009 (TIAM1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.88, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The independent human-brain map also detects TIAM1 with DLG4 residues 131–306. This supports association but does not establish a full-length physiological GEF-regulatory function. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The PPFIA1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q13136 (PPFIA1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.12299 to 0.019886), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Specify the independently supported GRIN2B partner class.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q13224 (GRIN2B; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.37, PDZ2=4.86, PDZ3=0. Independent controlled NR2B-tail and interaction-map assays establish this NMDA-receptor recognition mechanism; negative small-molecule inhibitor tests do not negate the positive receptor interface. The PDZ-domain/reagent measurements do not establish a native full-length complex, endogenous affinity or equivalent behavior of all DLG4 products.

Proposed replacements: ionotropic glutamate receptor binding

Summary: The CTBP1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q13363 (CTBP1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.11894 to 0.022996), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The AQP6 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q13520 (AQP6; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.055498 to 0.018901), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the DGKZ association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q13574 (DGKZ; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.7211979, PDZ2=4.9551531, PDZ3=3.83661831. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the MTMR1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q13613 (MTMR1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.21, PDZ2=4.7, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The ARHGEF7 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q14155-1 (ARHGEF7; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range 0.01928 to 0.025209), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the FZD2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q14332 (FZD2; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.84704489, PDZ2=4.9221943, PDZ3=4.24220707. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the KCNJ12 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q14500 (KCNJ12; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.22488325, PDZ2=4.55642065, PDZ3=4.31471098. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the FAT1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q14517 (FAT1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.41442565, PDZ2=4.80142606, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SCN5A association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q14524 (SCN5A; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.45566927, PDZ2=4.731512, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the KCNB1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q14721 (KCNB1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=4.0854157, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SLC17A1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q14916 (SLC17A1; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.82484421, PDZ2=4.03676532, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Specify the independently supported GRIN2C partner class.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q14957 (GRIN2C; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.6828158, PDZ2=5.32512959, PDZ3=3.77701987. Independent target-resolved NR2C-tail fluorescence-polarization/ELISA records support the same NMDA-receptor interface. No full-length affinity is inferred from the fragment measurements. The PDZ-domain/reagent measurements do not establish a native full-length complex, endogenous affinity or equivalent behavior of all DLG4 products.

Proposed replacements: ionotropic glutamate receptor binding

Summary: Specify the independently supported FRMPD4 partner class.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q14CM0 (FRMPD4; taxon 9606); maximum source COMP values by tested domain are PDZ1=5.04871461, PDZ2=5.59916477, PDZ3=5.25131075. Independent Preso/FRMPD4 interaction and spine-actin experiments establish the partner as a cytoskeletal regulator. The term describes binding that regulator, not actin-remodeling activity of DLG4. The PDZ-domain/reagent measurements do not establish a native full-length complex, endogenous affinity or equivalent behavior of all DLG4 products.

Proposed replacements: cytoskeletal regulatory protein binding

Summary: Retain the KARS1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q15046 (KARS1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.13287536, PDZ2=4.35358436, PDZ3=3.57691983. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the PLCB4 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q15147 (PLCB4; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.13096648, PDZ2=4.24573733, PDZ3=3.94768785. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the NECTIN1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q15223 (NECTIN1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.73211211, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Specify the independently supported ERBB4 partner class.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q15303 (ERBB4; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.87607252, PDZ2=4.96827769, PDZ3=4.23021007. Independent human-tail two-hybrid, rat-forebrain and controlled cellular assays establish ERBB4 recognition. The disputed PMID:16767099 disease-context result is not required for this refinement. The PDZ-domain/reagent measurements do not establish a native full-length complex, endogenous affinity or equivalent behavior of all DLG4 products.

Proposed replacements: receptor tyrosine kinase binding

Summary: Retain the RALBP1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q15311 (RALBP1; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.97224918, PDZ2=4.57643435, PDZ3=4.86756875. The selected nonzero composite supports the isolated PDZ–ligand interface. Separate phage-display and neuronal-fragment records support RALBP1 association. Its multiple GAP/scaffold roles do not by themselves identify the physiological function of this DLG4 interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the RPS6KA1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 12 sequence-supported measurement(s) for Q15418 (RPS6KA1; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.8, PDZ2=3.85, PDZ3=3.49. The selected nonzero composite supports the isolated PDZ–ligand interface. The source includes modified and unmodified RPS6KA1 reagents. The unmodified PDZ1 measurement has composite 3.67923818; the retained interaction is therefore not based solely on a phosphopeptide. This does not establish a DLG4 kinase-regulatory mechanism. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The NHERF2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q15599 (NHERF2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.04184 to 0.00728), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the TRIP6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q15654 (TRIP6; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.90918753, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SLC1A5 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q15758 (SLC1A5; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.55886104, PDZ2=0, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the EFNB3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q15768 (EFNB3; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.54174605, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The PKN2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q16513 (PKN2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.088417 to 0.024499), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the C3AR1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q16581 (C3AR1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.58189078, PDZ2=4.65013541, PDZ3=3.54040955. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The DUSP5 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q16690 (DUSP5; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.064515 to 0.027372), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The SLC5A12 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q1EHB4 (SLC5A12; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.11151 to 0.004493), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the PRR16 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q569H4 (PRR16; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.78205571, PDZ2=5.20249325, PDZ3=4.12270396. The selected nonzero composite supports the isolated PDZ–ligand interface. The neuronal map independently records PRR16 association, but the physiological function of that interface remains unresolved. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SDK2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q58EX2 (SDK2; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.24194104, PDZ2=4.4887391, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the SLC45A4 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q5BKX6 (SLC45A4; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.33169, PDZ2=4.59205745, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the XKR7 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q5GH72 (XKR7; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.93818811, PDZ2=4.91152891, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The CRB2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q5IJ48 (CRB2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range 0.0015819 to 0.020656), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The ZNF831 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q5JPB2 (ZNF831; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.04531 to 0.048308), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the IQSEC2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q5JU85 (IQSEC2; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.81778978, PDZ2=5.31254897, PDZ3=4.17853611. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The DGKK source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q5KSL6 (DGKK; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.019447 to 0.024244), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the SAPCD1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q5SSQ6 (SAPCD1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.47807465, PDZ2=4.52782253, PDZ3=4.5921791. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The PDZK1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q5T2W1 (PDZK1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.00434 to 0.02184), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The GPRC6A source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q5T6X5 (GPRC6A; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.055573 to 0.038536), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the ARHGEF16 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q5VV41 (ARHGEF16; taxon 9606); maximum source COMP values by tested domain are PDZ1=5.12500561, PDZ2=5.44432793, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ATRNL1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q5VV63 (ATRNL1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.3301385, PDZ2=4.43285596, PDZ3=3.87071177. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the TMEM215 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q68D42 (TMEM215; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.68, PDZ2=4.66, PDZ3=3.64. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The ARHGAP17 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q68EM7 (ARHGAP17; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range 0.00061949 to 0.041645), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The DENND5A source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6IQ26 (DENND5A; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.086687 to 0.046144), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The KCNV1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6PIU1 (KCNV1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.074462 to 0.041023), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the SLC2A7 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6PXP3 (SLC2A7; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=4.10698028, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The CSPG4 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6UVK1 (CSPG4; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range 0.011471 to 0.040614), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the KCNT2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6UVM3 (KCNT2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.62321392, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the KIRREL2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6UWL6 (KIRREL2; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.06483548, PDZ2=4.47681088, PDZ3=3.86430391. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The CES3 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6UWW8 (CES3; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.089715 to 0.018619), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the TMIGD1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6UXZ0 (TMIGD1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.78372797, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The DCHS2 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6V1P9 (DCHS2; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.08011 to 0.017863), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the NPSR1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6W5P4 (NPSR1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=3.49185152. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The PLEKHG7 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6ZR37 (PLEKHG7; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.053826 to 0.045552), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the RASSF6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6ZTQ3 (RASSF6; taxon 9606); maximum source COMP values by tested domain are PDZ1=5.03650552, PDZ2=5.47936249, PDZ3=4.39282736. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the GOLT1A association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q6ZVE7 (GOLT1A; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.04442921, PDZ2=4.71468156, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the RSRC2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q7L4I2 (RSRC2; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.49172018, PDZ2=0, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the NET1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q7Z628 (NET1; taxon 9606); maximum source COMP values by tested domain are PDZ1=5.20735135, PDZ2=5.76764534, PDZ3=4.91779595. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ORF putative E6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q81964 (ORF putative E6; taxon 37115); maximum source COMP values by tested domain are PDZ1=5.10591576, PDZ2=5.45149662, PDZ3=4.20967964. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the E6 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q82005 (E6; taxon 51033); maximum source COMP values by tested domain are PDZ1=3.96692603, PDZ2=4.13834805, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ADGRA1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q86SQ6 (ADGRA1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.99199611, PDZ2=5.08169623, PDZ3=4.60511899. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The MYPN source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q86TC9 (MYPN; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.022966 to 0.040857), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the MARCHF3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q86UD3 (MARCHF3; taxon 9606); maximum source COMP values by tested domain are PDZ1=5.4838791, PDZ2=6.03249026, PDZ3=4.93768507. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ZSCAN30 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q86W11 (ZSCAN30; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.59093259, PDZ2=4.9483022, PDZ3=4.21531111. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The UNC93A source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q86WB7 (UNC93A; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.075295 to -0.0024687), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the DGKH association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q86XP1 (DGKH; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.85150275, PDZ2=3.91825111, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the RNF130 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q86XS8 (RNF130; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.51340959, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The TRIM50 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q86XT4 (TRIM50; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.077472 to -0.0011704), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the MARCHF9 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q86YJ5 (MARCHF9; taxon 9606); maximum source COMP values by tested domain are PDZ1=5.05813444, PDZ2=5.27009156, PDZ3=4.80628349. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the PLEKHH2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8IVE3 (PLEKHH2; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.90971141, PDZ2=3.70406577, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The FMNL3 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8IVF7 (FMNL3; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.090267 to 0.028581), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the NOSTRIN association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8IVI9 (NOSTRIN; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=3.50341266. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The SLC22A9 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8IVM8 (SLC22A9; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.15696 to 0.0076471), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the TMEM151B association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8IW70 (TMEM151B; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.97872211, PDZ2=4.58582585, PDZ3=4.10700362. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the ADGRA3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8IWK6 (ADGRA3; taxon 9606); maximum source COMP values by tested domain are PDZ1=5.21027861, PDZ2=5.41393063, PDZ3=4.93644403. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The SCN4B source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8IWT1 (SCN4B; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.0028669 to 0.039853), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The AMOTL1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8IY63 (AMOTL1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.14056 to 0.0046505), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the ABCA7 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8IZY2 (ABCA7; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.69711357, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the NLGN4X association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8N0W4 (NLGN4X; taxon 9606); maximum source COMP values by tested domain are PDZ1=3.5135919, PDZ2=3.97488658, PDZ3=4.03889104. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the DOCK4 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8N1I0 (DOCK4; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=3.68962198. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the LNX2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8N448 (LNX2; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.44, PDZ2=4.36, PDZ3=3.58. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The SH2D3C source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8N5H7 (SH2D3C; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.044091 to 0.031879), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The CLDN19 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8N6F1 (CLDN19; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.067769 to -0.005553), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the KIR3DL3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8N743 (KIR3DL3; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.03601652, PDZ2=4.21942624, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the TMEM178A association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8NBL3 (TMEM178A; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.33523612, PDZ2=4.61018738, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the LSM14A association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8ND56-2 (LSM14A; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=3.70866812, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The TNRC6A source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8NDV7 (TNRC6A; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.031025 to 0.031728), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The GARIN6 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8NEG0 (GARIN6; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range 0.0058261 to 0.043044), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the TRPV3 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8NET8 (TRPV3; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.35563093, PDZ2=4.40257652, PDZ3=4.19889165. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The GOT1L1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8NHS2 (GOT1L1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.071247 to 0.030826), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the GAS2L2 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8NHY3 (GAS2L2; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.03406325, PDZ2=4.68891322, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the VANGL1 association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8TAA9 (VANGL1; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.39955355, PDZ2=4.70844033, PDZ3=4.51441237. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: Retain the FAM110D association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8TAY7 (FAM110D; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.83461773, PDZ2=5.62643418, PDZ3=4.42439748. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.

Summary: The LNX1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8TBB1 (LNX1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.03652 to 0.03091), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: The SHKBP1 source-pair assertion remains unresolved at the recovered measurement level.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8TBC3 (SHKBP1; taxon 9606); maximum source COMP values by tested domain are PDZ1=0, PDZ2=0, PDZ3=0. The selected DAPF records are below the normalized binding-intensity quantification threshold of 0.05 (range -0.01141 to 0.02682), and none has a positive matched fluorescence-polarization measurement. Their zero composite is a censored assay result, not zero affinity. Negative binding intensities represent no measurable depletion relative to the control and experimental noise, not negative affinity. The original study explicitly cautions that below-threshold pairs are not demonstrated noninteractions. The imported positive IPI assertion is preserved, but binding for these specific fragments remains unquantified; neither a credible positive interface nor absence of binding is established. Retain source-specific uncertainty without inferring a native full-length role.

Summary: Retain the FAM110B association with its measured fragment scope.

Reason: The published SD1 workbook resolves 3 sequence-supported measurement(s) for Q8TC76 (FAM110B; taxon 9606); maximum source COMP values by tested domain are PDZ1=4.06212909, PDZ2=4.52942106, PDZ3=0. The selected nonzero composite supports the isolated PDZ–ligand interface. The assay does not establish the physiological role of the full-length pair. Retain positive binding without naming a free-peptide biological function or importing an enzymatic/receptor subclass solely from the partner identity.