DLG3

Summary: Calcium-dependent calmodulin binding is demonstrated.

Reason: The actual original tests human DLG3 constructs and purified bovine brain calmodulin, including surface plasmon resonance and calcium dependence. The 44 nM affinity and mapped basic region support calmodulin binding. Preserve the bovine partner identity P62157; this is not an assay of every human DLG3 product.

Proposed replacements: calmodulin binding

Summary: DLG3 recognizes an NMDA receptor tail.

Reason: The original tests human DLG3 and a rat NR2B C-terminal peptide, with a terminal-valine deletion control. This supports ionotropic glutamate receptor binding, without claiming that the historical rat peptide was a full-length human Q13224 construct. The conserved receptor-recognition role is independently supported by the core literature.

Proposed replacements: ionotropic glutamate receptor binding

Summary: DLG3 binds the receptor tyrosine kinase ERBB4.

Reason: The original human-brain yeast two-hybrid screen uses the human ERBB4 C-terminal 238 residues and identifies SAP102. The receptor-tyrosine-kinase partner class supports the refinement. The later co-immunoprecipitation emphasized PSD-95 and is not relabeled as a DLG3 experiment.

Proposed replacements: receptor tyrosine kinase binding

Summary: Retain the curated LRP2 association with its domain-assay scope.

Reason: The accessible abstract explicitly reports megalin binding by SAP102 PDZ2, and the exact IntAct pair records specify domain/peptide experiments. Full original recovery failed. Retain this positive curator-backed interaction; do not transfer the PSD-95 cellular localization/co-immunoprecipitation experiments to DLG3 or infer a signaling-receptor role for endocytic LRP2.

Summary: ABCA1-tail recognition is retained as a non-core association.

Reason: The curated PMID:16192269 peptide-array record specifies an ABCA1 tail and DLG3 PDZ fragments; its original remains abstract-only. Independently read PMID:36115835 SD1 reports positive recognition of the corresponding ABCA1 peptide. Retain the supported fragment association without inferring ATPase regulation, a full-length membrane complex, or direct verification of the unavailable 2005 Methods. A generic peptide-binding replacement would describe the assay reagent without establishing a more informative biological role.

Summary: DLG3 binds the spine regulator FRMPD4/Preso.

Reason: The original human Preso C-terminal motif and terminal-valine mutant establish PDZ-dependent recognition by SAP102. Figure 1 also reports pull-down, HEK293T co-immunoprecipitation and rat-brain complexes with PSD-95-family proteins including SAP102. Independently, Preso regulates spine density and spine filamentous actin. GO:0005519 describes binding to a protein that modulates cytoskeletal reorganization, so this partner class is supported beyond the presence of a PDZ-binding motif. It does not imply that DLG3 binds the FERM domain or reproduces the PSD-95-specific localization effects.

Proposed replacements: cytoskeletal regulatory protein binding

Summary: The PPP1CA association supports phosphatase binding.

Reason: The original 19389623 cache remains abstract-only, so its detailed assay is not claimed as independently read. The curated literal PPP1CA pair is consistent with the existing phosphatase-binding annotation and the separately read Dlg3–PP1 complex in PMID:21920314. Refine the established phosphatase partner class without attributing phosphatase catalysis to DLG3.

Proposed replacements: phosphatase binding

Summary: DLG3 recognizes the GPR85 receptor tail.

Reason: The actual original tests a GST fusion of the GPR85 C-terminal 11 residues against a terminal-motif deletion, with mouse brain and transfected-cell association assays. GPR85 is a G protein-coupled receptor, supporting this partner-class refinement. Host cells do not by themselves establish construct species, and this does not assign an agonist function to DLG3.

Proposed replacements: G protein-coupled receptor binding

Summary: DLG3 recognizes a GluN2C receptor-tail motif.

Reason: PMID:30126976 tests nine-residue human tails against human DLG3 PDZ2, using native and Ser/Thr-to-Glu phosphomimetic libraries. The exact GRIN2C pair and positive native-tail holdup measurements in PMID:36115835 support the same ionotropic-glutamate-receptor recognition class as the independently established DLG3–GluN2 mechanism. Retain the fragment scope: neither pair-specific phosphorylation dependence nor a full-length native GRIN2C complex was demonstrated by this screen.

Proposed replacements: ionotropic glutamate receptor binding

Summary: DLG3 recognizes a motif of the cytoskeletal regulator FRMPD4.

Reason: The human DLG3 PDZ2 phage screen in PMID:30126976 includes the FRMPD4 tail. Independent native-tail holdup measurements and PMID:19118189 Fig. 1 support this pair: the latter explicitly includes SAP102 in motif-dependent interactions and rat-brain complexes, and establishes Preso/FRMPD4 as a regulator of dendritic spine morphology. Refine to cytoskeletal regulatory protein binding without assigning FRMPD4 activity to DLG3 or claiming every phage hit forms a native complex.

Proposed replacements: cytoskeletal regulatory protein binding

Summary: NET1-tail recognition is retained as a non-core association.

Reason: The human DLG3 PDZ2 phage screen identifies the NET1 tail, and independent holdup measurements support native-tail recognition. The screen includes phosphomimetic variants; their presence alone does not establish physiological phosphorylation dependence. Retain this supported fragment association without inferring full-length native binding or a GEF-regulatory role for DLG3. A generic peptide-binding replacement adds assay-format information rather than an established biological function.

Summary: CYSLTR2-tail recognition is retained as a non-core association.

Reason: The human DLG3 PDZ2 phage screen and independent holdup measurements support recognition of a CYSLTR2-derived tail peptide. Retain this fragment association as non-core. The isolated motif experiments do not establish full-length native receptor association or a receptor-regulatory role, and a generic peptide-binding replacement merely restates the synthetic ligand format.

Summary: Retain the positive HuRI association with vitronectin.

Reason: HuRI reports the DLG3–VTN pair in array, prey-pooling and validated-two-hybrid records from the same study. Sequence checksums authenticate 817-aa human DLG3 and 478-aa vitronectin; these records support binary binding capacity rather than three independent physiological replications. Retain the positive association as non-core. Vitronectin is an established adhesion molecule, but the examined evidence does not resolve this pair in its native extracellular context or establish an adhesion-related function for DLG3. A class-specific functional refinement is therefore not adopted here; the interaction itself is not rejected.

Summary: Retain the binary KDELR1 interaction.

Reason: HuRI pair records and sequence checksums authenticate DLG3 and KDELR1. KDELR1 is a retrieval receptor; this alone does not establish a signaling-receptor-binding subclass or that DLG3 participates in ER retrieval. Retain the experimentally supported binary association under the project binding policy.

Summary: Retain the binary RPS8 interaction.

Reason: HuRI authenticates the DLG3–RPS8 pair and both current sequences. RPS8 is a ribosomal protein, but binding one protein does not establish binding to an assembled RNA–protein complex or ribosome. Retain the binary interaction without those broader complex/function claims.

Summary: Retain the positive HuRI association with EIF4H-2.

Reason: HuRI array, prey-pooling and validated-two-hybrid records authenticate human DLG3 and the 228-aa EIF4H-2 product. Their cytoplasmic locations are compatible and are not evidence against binding. The study establishes binary interaction capacity, while the native cellular role of this particular pair remains unresolved. Retain the supported association as non-core without promoting a translation-related functional subclass solely from the partner identity or assigning translational regulation to DLG3. No other DLG3 product is inferred from the assay.

Summary: Retain the Q6IS01 binary association.

Reason: The three HuRI records and sequence checksum identify the literal 543-aa Q6IS01 product. Its DLGAP1 annotation does not justify replacing the accession with another canonical product or assuming an assembled scaffold complex. Retain the supported pair without an unsupported narrower recognition class.

Summary: Retain binding to the short DHRS11 product.

Reason: HuRI checksums match Q6UWP2-2, a 181-aa product missing the canonical N-terminal 79 residues, and 817-aa DLG3. Catalytic activity established for full-length DHRS11 is not automatically established for this short assayed product. Retain the pair without an enzyme-binding refinement based only on the full-length protein name.

Summary: Retain the OSBP2-2 binary association.

Reason: HuRI records and sequence checksums identify the 915-aa OSBP2-2 product. Its lipid-transfer class does not establish an enzyme or a more specific recognition mechanism in this assay. Retain the supported interaction without assigning lipid transport to DLG3.

Summary: Retain the PLEKHA2 binary association.

Reason: HuRI authenticates DLG3 and PLEKHA2 sequences. PLEKHA2 lipid-binding/recruitment annotations do not establish a narrower recognized protein class here. Independent peptide binding is compatible with the association but does not convert this full-product binary record into a membrane-signaling assay.

Summary: Retain the DLGAP2-3 binary association.

Reason: The exact HuRI pair uses the 975-aa DLGAP2-3 product and canonical DLG3, with matching sequence checksums. Retain this interaction without inferring a complete postsynaptic complex, physiological stoichiometry, or a more specific partner-recognition activity from the DLGAP name.

Summary: Retain the KCNA4 co-complex association.

Reason: The exact BioPlex anti-tag affinity-purification record supports DLG3 association with KCNA4. The original workflow aggregates proteins at gene level and reports co-complex edges; it does not establish direct ion-channel recognition, physiological regulation, or an exact assayed DLG3 isoform. Retain the positive association without a narrower binding MF based solely on the channel class.

Summary: Retain the ARHGAP17 co-complex association.

Reason: BioPlex IntAct EBI-54784725 and the independently verified primary AP-MS graph edge 609986 in PMID:40205054 support the same association. The 2022 isolated PDZ-tail assays are below detection. Neither AP-MS hit establishes direct recognition of a cytoskeletal regulator or GAP inhibition by DLG3, so retain the association without that MF refinement.

Summary: Retain the ARHGEF26 co-complex association.

Reason: The exact BioPlex record EBI-54784725 is a spoke-expanded ARHGEF26–DLG3 pair, distinct from the ARHGAP17 pair sharing that interaction accession. AP-MS supports association, not necessarily direct recognition. Known cytoskeletal regulation by ARHGEF26 does not alone establish a class-specific DLG3 binding mechanism.

Summary: Retain the DLGAP4 co-complex association.

Reason: BioPlex IntAct EBI-54638731 supports association with DLGAP4. The separate PDZ-tail screen is below detection and does not negate an association through other regions or complex components. Retain the supported co-complex interaction without assigning a demonstrated PDZ-tail mechanism or stable complex stoichiometry.

Summary: The literal REELD1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for REELD1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 41344, 49039, 51774 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a TTC24-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the TTC24-derived synthetic peptide biotin-ado-ado-PMESGICTIV, with composite pKd 4.8861552 (sheet row 2259). The sequence crosswalk retains the literal A2A3L6 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a E6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the E6-derived synthetic peptide biotin-ttds-SRPQRTQTQV, with composite pKd 5.058141 (sheet row 1645). The sequence crosswalk retains the literal A4U7F2 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal GAGE12J pair remains unresolved at the measured scope.

Reason: The original SD1 rows 9021, 55785 and 64021 test the synthetic GAGE12J-labeled peptide PEEGKKQSQC. Row 9021 gives positive DLG3_2 DAPF/composite binding, pKd 4.03522737; the other two domain measurements are below threshold. The corresponding current A6NER3 sequence is PEEGEKQSQC, with an E in place of K. Preserve the positive measured peptide result, but its mapping to the literal current A6NER3 product remains unresolved. This is not a wholly undetected pair or a claim of biological noninteraction/paralog misattribution.

Summary: DLG3 PDZ-domain binding to a SMCHD1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SMCHD1-derived synthetic peptide biotin-ado-ado-QNRIITKTDV, with composite pKd 4.0760213 (sheet row 8511). The sequence crosswalk retains the literal A6NHR9 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a KCNJ18-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the KCNJ18-derived synthetic peptide biotin-ado-ado-QRPYRRGSEI, with composite pKd 4.1364888 (sheet row 7765). The sequence crosswalk retains the literal B7U540 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal PPP1R3G pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for PPP1R3G are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 42229, 50591, 53473 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a TMEM178B-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the TMEM178B-derived synthetic peptide biotin-ado-ado-KSRPENGTVC, with composite pKd 3.5445828 (sheet row 16724). The sequence crosswalk retains the literal H3BS89 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a E-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the E-derived synthetic peptide biotin-DSKPPLPPDEWV, with composite pKd 3.9598992 (sheet row 9983). The sequence crosswalk retains the literal K9N5R3 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a CCL24-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CCL24-derived synthetic peptide biotin-ado-ado-QRYPGNQTTC, with composite pKd 4.2641298 (sheet row 6409). The sequence crosswalk retains the literal O00175 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ARVCF-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ARVCF-derived synthetic peptide Biotin-Ahx-AKPQPVDSWV, with composite pKd 4.49 (sheet row 4478). The sequence crosswalk retains the literal O00192 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SLC1A7-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SLC1A7-derived synthetic peptide biotin-ado-ado-IQISELETNV, with composite pKd 4.6555451 (sheet row 3447). The sequence crosswalk retains the literal O00341 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a CCRL2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CCRL2-derived synthetic peptide biotin-ado-ado-REEPDHSTEV, with composite pKd 4.5852897 (sheet row 3894). The sequence crosswalk retains the literal O00421 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a DLL1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the DLL1-derived synthetic peptide Biotin-Ahx-KDECVIATEV, with composite pKd 4.52 (sheet row 4286). The sequence crosswalk retains the literal O00548 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a CACNA1A-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CACNA1A-derived synthetic peptide biotin-ado-ado-PYSESDDDWC, with composite pKd 4.1600253 (sheet row 7509). The sequence crosswalk retains the literal O00555 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal PODXL pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for PODXL are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 27015, 27016, 27017 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a CES2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CES2-derived synthetic peptide biotin-ado-ado-EEPEERHTEL, with composite pKd 4.3813835 (sheet row 5336). The sequence crosswalk retains the literal O00748 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal CLDN4 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CLDN4 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 50485, 57288, 63398 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a CIT-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the CIT-derived synthetic peptide biotin-ttds-VNKVWDQSSV, with composite pKd 3.6966542 (sheet row 13918). The sequence crosswalk retains the literal O14578 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal NHERF1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for NHERF1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 25881, 25882, 25883 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a RGS12-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the RGS12-derived synthetic peptide Biotin-Ahx-KTSAHHATFV, with composite pKd 3.92 (sheet row 10494). The sequence crosswalk retains the literal O14924 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a TECPR2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the TECPR2-derived synthetic peptide biotin-ado-ado-EDLEDEWEVI, with composite pKd 4.0910475 (sheet row 8328). The sequence crosswalk retains the literal O15040 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a AXIN1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the AXIN1-derived synthetic peptide Biotin-GSGSGS-TLSLTDSSVDGIPPYR-CONH2, with composite pKd 4.0805707 (sheet row 8454). The sequence crosswalk retains the literal O15169 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal EPHB6 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for EPHB6 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 51550, 52691, 60245 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a SLC16A3-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the SLC16A3-derived synthetic peptide biotin-ttds-EVVHTPETSV, with composite pKd 4.2805224 (sheet row 6259). The sequence crosswalk retains the literal O15427 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a CLDN3-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the CLDN3-derived synthetic peptide biotin-ado-ado-GTGYDRKDYV, with composite pKd 3.6381224 (sheet row 14910). The sequence crosswalk retains the literal O15551 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a PLXNB1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the PLXNB1-derived synthetic peptide biotin-ado-ado-AAVENKVTDL, with composite pKd 3.7172933 (sheet row 13538). The sequence crosswalk retains the literal O43157 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ARHGAP6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ARHGAP6-derived synthetic peptide biotin-ttds-NPDALPETLV, with composite pKd 4.1797981 (sheet row 7285). The sequence crosswalk retains the literal O43182 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a GRID2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GRID2-derived synthetic peptide biotin-ado-ado-GNDPDRGTSI, with composite pKd 4.2454935 (sheet row 6596). The sequence crosswalk retains the literal O43424 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a AKAP10-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the AKAP10-derived synthetic peptide biotin-ado-ado-DQPLEKSTKL, with composite pKd 4.1358104 (sheet row 7772). The sequence crosswalk retains the literal O43572 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal PRKN pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for PRKN are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 47472, 47571, 53170 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a EVI5-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the EVI5-derived synthetic peptide biotin-ado-ado-RRRESYSTTV, with composite pKd 5.4382796 (sheet row 804). The sequence crosswalk retains the literal O60447 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SLC16A7-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SLC16A7-derived synthetic peptide biotin-ado-ado-SVTSERETNI, with composite pKd 4.24594 (sheet row 6585). The sequence crosswalk retains the literal O60669 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal LPXN pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for LPXN are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 37804, 41233, 43922 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal CYTIP pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CYTIP are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 27235, 27236, 27237 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal RAMP3 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for RAMP3 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 39619, 59960, 60167 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a NOS1AP-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the NOS1AP-derived synthetic peptide biotin-ado-ado-GDGLDDEIAV, with composite pKd 4.0108678 (sheet row 9295). The sequence crosswalk retains the literal O75052 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SDC3-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SDC3-derived synthetic peptide biotin-ado-ado-KPDKQEEFYA, with composite pKd 4.0509299 (sheet row 8818). The sequence crosswalk retains the literal O75056 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a FZD7-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the FZD7-derived synthetic peptide biotin-ttds-SHSSKGETAV, with composite pKd 4.5289565 (sheet row 4249). The sequence crosswalk retains the literal O75084 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a BANF1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the BANF1-derived synthetic peptide biotin-ado-ado-CLREWCDAFL, with composite pKd 4.15427 (sheet row 7584). The sequence crosswalk retains the literal O75531 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a STK16-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the STK16-derived synthetic peptide biotin-ado-ado-PAPGQHTTQI, with composite pKd 4.1103553 (sheet row 8083). The sequence crosswalk retains the literal O75716 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal SLC22A3 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for SLC22A3 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 41216, 48898, 57263 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a CIB2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CIB2-derived synthetic peptide biotin-ado-ado-DFLSTFHIRI, with composite pKd 3.9666109 (sheet row 9897). The sequence crosswalk retains the literal O75838 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a DGKI-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the DGKI-derived synthetic peptide biotin-ado-ado-IGHEDLETAV, with composite pKd 4.8047549 (sheet row 2631). The sequence crosswalk retains the literal O75912 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a FCHSD2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the FCHSD2-derived synthetic peptide biotin-ado-ado-KIEDVEITLV, with composite pKd 3.532968 (sheet row 16953). The sequence crosswalk retains the literal O94868 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal SLCO2B1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for SLCO2B1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 50658, 58799, 62956 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a SBF1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SBF1-derived synthetic peptide biotin-ado-ado-DRIQSCLSDA, with composite pKd 4.1930776 (sheet row 7131). The sequence crosswalk retains the literal O95248 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal ABCC6 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for ABCC6 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 34954, 53944, 58869 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal CLDN7 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CLDN7 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 36972, 56772, 56979 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a ABCA1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ABCA1-derived synthetic peptide Biotin-Ahx-QDEKVKESYV, with composite pKd 4.92 (sheet row 2110). The sequence crosswalk retains the literal O95477 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal CLDN9 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CLDN9 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 35257, 51548, 52257 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal CLDN14 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CLDN14 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 36876, 45940, 49949 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a SEMA4F-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SEMA4F-derived synthetic peptide biotin-ado-ado-PLATCDETSI, with composite pKd 4.299449 (sheet row 6090). The sequence crosswalk retains the literal O95754 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal CLDN1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CLDN1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 36626, 46377, 50083 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a TGFA-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the TGFA-derived synthetic peptide biotin-ado-ado-TACCHSETVV, with composite pKd 4.7392411 (sheet row 2945). The sequence crosswalk retains the literal P01135 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a E6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the E6-derived synthetic peptide biotin-ttds-SSRTRRETQL, with composite pKd 4.8828976 (sheet row 2273). The sequence crosswalk retains the literal P03126 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a Tax-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the Tax-derived synthetic peptide biotin-ttds-SEKHFRETEV, with composite pKd 5.561441 (sheet row 651). The sequence crosswalk retains the literal P03409 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a MAS1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the MAS1-derived synthetic peptide biotin-ttds-CNTVTVETVV, with composite pKd 4.5329755 (sheet row 4219). The sequence crosswalk retains the literal P04201 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ERBB2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ERBB2-derived synthetic peptide biotin-ado-ado-PEYLGLDVPV, with composite pKd 3.5266306 (sheet row 17099). The sequence crosswalk retains the literal P04626 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a GYPC-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GYPC-derived synthetic peptide biotin-ado-ado-GDSSRKEYFI, with composite pKd 4.1854797 (sheet row 7210). The sequence crosswalk retains the literal P04921 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a E6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the E6-derived synthetic peptide biotin-ttds-SRSRRRETAL, with composite pKd 5.069285 (sheet row 1609). The sequence crosswalk retains the literal P06427 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a E6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the E6-derived synthetic peptide biotin-ttds-RLQRRRETQV, with composite pKd 5.457669 (sheet row 784). The sequence crosswalk retains the literal P06463 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal ADRB2 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for ADRB2 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 22256, 22257, 22258 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a IGF1R-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the IGF1R-derived synthetic peptide biotin-ado-ado-ALPLPQSSTC, with composite pKd 4.2238794 (sheet row 6811). The sequence crosswalk retains the literal P08069 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal PFKM pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for PFKM are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 49041, 59812, 64754 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal PDGFRB pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for PDGFRB are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 39102, 55801, 58592 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a TMEM225B-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the TMEM225B-derived synthetic peptide biotin-ado-ado-ETQVTAETVI, with composite pKd 4.4266192 (sheet row 4990). The sequence crosswalk retains the literal P0DP42 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a POLR1D-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the POLR1D-derived synthetic peptide biotin-ado-ado-QKASRNESTF, with composite pKd 4.2281401 (sheet row 6765). The sequence crosswalk retains the literal P0DPB6 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal E pair remains unresolved at the measured scope.

Reason: discordant assays: LYSC PDZ2 pKd4.09810075, composite DAPF all zero. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 21138, 21139, 21885 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal KIT pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for KIT are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 41956, 44475, 45210 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal HSPA5 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for HSPA5 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 45153, 58150, 59696 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a SLC2A1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SLC2A1-derived synthetic peptide biotin-ttds-FHPLGADSQV, with composite pKd 4.0317897 (sheet row 9059). The sequence crosswalk retains the literal P11166 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SLC2A3-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SLC2A3-derived synthetic peptide biotin-ado-ado-EPAKETTTNV, with composite pKd 4.1480675 (sheet row 7655). The sequence crosswalk retains the literal P11169 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a BCR-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the BCR-derived synthetic peptide biotin-ado-ado-RQSILFSTEV, with composite pKd 4.7913317 (sheet row 2693). The sequence crosswalk retains the literal P11274 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal SRC pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for SRC are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 44502, 50015, 60276 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal CFTR pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CFTR are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 23146, 23147, 23148 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a NCF1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the NCF1-derived synthetic peptide biotin-ado-ado-STKRKLASAV, with composite pKd 4.448701 (sheet row 4798). The sequence crosswalk retains the literal P14598 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a JUP-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the JUP-derived synthetic peptide biotin-ado-ado-PYPTADHMLA, with composite pKd 4.0505794 (sheet row 8824). The sequence crosswalk retains the literal P14923 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a CD46-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CD46-derived synthetic peptide biotin-ado-ado-THREVKFTSL, with composite pKd 4.2279626 (sheet row 6769). The sequence crosswalk retains the literal P15529 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ATP2A2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ATP2A2-derived synthetic peptide biotin-ado-ado-YLEPVLSSEL, with composite pKd 4.1811179 (sheet row 7265). The sequence crosswalk retains the literal P16615-3 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal GJA1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for GJA1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 35878, 40792, 43653 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a E6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the E6-derived synthetic peptide biotin-ttds-SRRPRTETQV, with composite pKd 5.413425 (sheet row 841). The sequence crosswalk retains the literal P17386 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a PRKACA-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the PRKACA-derived synthetic peptide biotin-ado-ado-EKCGKEFSEF, with composite pKd 4.1055773 (sheet row 8144). The sequence crosswalk retains the literal P17612 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a TYRP1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the TYRP1-derived synthetic peptide biotin-ado-ado-KLQNPNQSVV, with composite pKd 3.862608 (sheet row 11318). The sequence crosswalk retains the literal P17643 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a KCNA6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the KCNA6-derived synthetic peptide biotin-ado-ado-YAEKRMLTEV, with composite pKd 4.5980583 (sheet row 3812). The sequence crosswalk retains the literal P17658 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ATP2B1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ATP2B1-derived synthetic peptide biotin-ttds-SPLHSLETSL, with composite pKd 4.3450913 (sheet row 5668). The sequence crosswalk retains the literal P20020 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a NEB-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the NEB-derived synthetic peptide biotin-ado-ado-MLPANYVEAI, with composite pKd 4.1108945 (sheet row 8078). The sequence crosswalk retains the literal P20929 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a KCNA4-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the KCNA4-derived synthetic peptide biotin-ttds-SNAKAVETDV, with composite pKd 5.2329335 (sheet row 1170). The sequence crosswalk retains the literal P22459 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a KCNA5-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the KCNA5-derived synthetic peptide biotin-ttds-CLDTSRETDL, with composite pKd 4.3492927 (sheet row 5631). The sequence crosswalk retains the literal P22460 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a UQCRC2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the UQCRC2-derived synthetic peptide biotin-ado-ado-LGHTPFVDEL, with composite pKd 3.4788516 (sheet row 18177). The sequence crosswalk retains the literal P22695 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a PTPRG-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the PTPRG-derived synthetic peptide biotin-ado-ado-DPAESMESLV, with composite pKd 4.7169776 (sheet row 3063). The sequence crosswalk retains the literal P23470 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a PTPRZ1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the PTPRZ1-derived synthetic peptide biotin-ado-ado-NIAESLESLV, with composite pKd 4.8118567 (sheet row 2605). The sequence crosswalk retains the literal P23471 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a MCC-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the MCC-derived synthetic peptide biotin-ado-ado-SRPHTNETSL, with composite pKd 3.947474 (sheet row 10137). The sequence crosswalk retains the literal P23508 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ATP2B4-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ATP2B4-derived synthetic peptide biotin-ttds-SSLQSLETSV, with composite pKd 5.1998572 (sheet row 1268). The sequence crosswalk retains the literal P23634 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal CXCR1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CXCR1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 43973, 46405, 54158 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a APC-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the APC-derived synthetic peptide Biotin-Ahx-HSGSYLVTSV, with composite pKd 5.07 (sheet row 1605). The sequence crosswalk retains the literal P25054 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ADRA1D-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ADRA1D-derived synthetic peptide biotin-ado-ado-DYSNLRETDI, with composite pKd 4.3895071 (sheet row 5270). The sequence crosswalk retains the literal P25100 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a CTNNA2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CTNNA2-derived synthetic peptide biotin-ado-ado-LSEFKAMDSF, with composite pKd 4.1591658 (sheet row 7533). The sequence crosswalk retains the literal P26232 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal U2AF2 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for U2AF2 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 45106, 52161, 63076 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a E6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the E6-derived synthetic peptide biotin-ttds-RTRQRNETQV, with composite pKd 5.0998977 (sheet row 1521). The sequence crosswalk retains the literal P26554 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal ACVR2A pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for ACVR2A are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 22161, 22162, 22163 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a E6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the E6-derived synthetic peptide biotin-ttds-SKPTRRETEV, with composite pKd 5.4916269 (sheet row 742). The sequence crosswalk retains the literal P27228 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a MAP4-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the MAP4-derived synthetic peptide biotin-ttds-LDSQIQETSI, with composite pKd 3.9324577 (sheet row 10342). The sequence crosswalk retains the literal P27816 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a HTR2A-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the HTR2A-derived synthetic peptide biotin-ado-ado-DGVNEKVSCV, with composite pKd 4.8180502 (sheet row 2577). The sequence crosswalk retains the literal P28223 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a HTR2C-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the HTR2C-derived synthetic peptide biotin-ado-ado-SVVSERISSV, with composite pKd 4.6769211 (sheet row 3319). The sequence crosswalk retains the literal P28335 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SDC4-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SDC4-derived synthetic peptide biotin-ado-ado-KKAPTNEFYA, with composite pKd 4.1421837 (sheet row 7706). The sequence crosswalk retains the literal P31431 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a GUCY1A2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the GUCY1A2-derived synthetic peptide biotin-ado-ado-GTMFLRETSL, with composite pKd 4.6420239 (sheet row 3525). The sequence crosswalk retains the literal P33402 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a MCM7-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the MCM7-derived synthetic peptide biotin-ado-ado-NASRTRITFV, with composite pKd 4.7488255 (sheet row 2896). The sequence crosswalk retains the literal P33993 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SDC2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SDC2-derived synthetic peptide biotin-ado-ado-QKAPTKEFYA, with composite pKd 4.1760341 (sheet row 7324). The sequence crosswalk retains the literal P34741 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a CRHR1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CRHR1-derived synthetic peptide biotin-ado-ado-FHSIKQSTAV, with composite pKd 4.6052671 (sheet row 3760). The sequence crosswalk retains the literal P34998 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a CTNNA1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CTNNA1-derived synthetic peptide biotin-ado-ado-LSEFKAMDSI, with composite pKd 3.5640051 (sheet row 16323). The sequence crosswalk retains the literal P35221 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal CTNNB1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CTNNB1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 23648, 23649, 23650 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a NF2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_1 binding to the NF2-derived synthetic peptide biotin-ado-ado-KSRVAFFEEL, with composite pKd 3.5776995 (sheet row 16042). The sequence crosswalk retains the literal P35240-1 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SSTR5-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SSTR5-derived synthetic peptide biotin-ado-ado-ANGLMQTSKL, with composite pKd 3.7450588 (sheet row 13078). The sequence crosswalk retains the literal P35346 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SCN4A-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SCN4A-derived synthetic peptide biotin-ado-ado-VRPGVKESLV, with composite pKd 4.9980196 (sheet row 1824). The sequence crosswalk retains the literal P35499 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ACTN2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ACTN2-derived synthetic peptide biotin-ado-ado-SSALYGESDL, with composite pKd 4.1761305 (sheet row 7323). The sequence crosswalk retains the literal P35609 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a GJC1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GJC1-derived synthetic peptide biotin-ado-ado-SGDGKTSVWI, with composite pKd 4.1588543 (sheet row 7537). The sequence crosswalk retains the literal P36383 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a MAP2K2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the MAP2K2-derived synthetic peptide biotin-ttds-QPGTPTRTAV, with composite pKd 3.9325673 (sheet row 10339). The sequence crosswalk retains the literal P36507 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a L2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the L2-derived synthetic peptide Biotin-Ahx-RRRKRKRTYL, with composite pKd 4.28 (sheet row 6269). The sequence crosswalk retains the literal P36762 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a E6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the E6-derived synthetic peptide biotin-ttds-RHTTSTETAV, with composite pKd 5.4054085 (sheet row 860). The sequence crosswalk retains the literal P36809 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SLC26A3-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SLC26A3-derived synthetic peptide biotin-ado-ado-VYEVPVETKF, with composite pKd 4.1295309 (sheet row 7851). The sequence crosswalk retains the literal P40879 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a GRM5-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GRM5-derived synthetic peptide biotin-ado-ado-RDYTQSSSSL, with composite pKd 3.96499 (sheet row 9920). The sequence crosswalk retains the literal P41594 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a GRIA2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GRIA2-derived synthetic peptide biotin-ado-ado-NVYGIESVKI, with composite pKd 4.1853685 (sheet row 7213). The sequence crosswalk retains the literal P42262 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal GRIA3 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for GRIA3 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 43596, 49658, 64970 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal SLC1A3 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for SLC1A3 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 35624, 41788, 47457 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a SLC1A1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SLC1A1-derived synthetic peptide biotin-ado-ado-TISFTQTSQF, with composite pKd 4.0785664 (sheet row 8477). The sequence crosswalk retains the literal P43005 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SLC1A4-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SLC1A4-derived synthetic peptide biotin-ado-ado-PELESKESVL, with composite pKd 3.7888797 (sheet row 12397). The sequence crosswalk retains the literal P43007 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a PTGIR-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the PTGIR-derived synthetic peptide biotin-ado-ado-AEASVACSLC, with composite pKd 3.6940752 (sheet row 13955). The sequence crosswalk retains the literal P43119 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a GRK6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GRK6-derived synthetic peptide biotin-ado-ado-DSEEELPTRL, with composite pKd 3.6642258 (sheet row 14440). The sequence crosswalk retains the literal P43250 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal GPR6 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for GPR6 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 24216, 24217, 24218 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal SLCO1A2 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for SLCO1A2 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 38249, 44444, 50363 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal YAP1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for YAP1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 45856, 55860, 60553 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a GPR12-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GPR12-derived synthetic peptide biotin-ado-ado-AQRARSPSDV, with composite pKd 4.3190178 (sheet row 5906). The sequence crosswalk retains the literal P47775 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a MTNR1A-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the MTNR1A-derived synthetic peptide biotin-ado-ado-NNNVVKVDSV, with composite pKd 4.032957 (sheet row 9046). The sequence crosswalk retains the literal P48039 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a KCNJ1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the KCNJ1-derived synthetic peptide biotin-ado-ado-EVNETDDTKM, with composite pKd 3.6306197 (sheet row 15038). The sequence crosswalk retains the literal P48048 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a KCNJ4-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the KCNJ4-derived synthetic peptide biotin-ado-ado-NISYRRESAI, with composite pKd 4.3480638 (sheet row 5643). The sequence crosswalk retains the literal P48050 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal SLC9A3 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for SLC9A3 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 43767, 45739, 56403 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal ADGRE5 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for ADGRE5 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 45452, 49866, 52901 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal PTH2R pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for PTH2R are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 36359, 47192, 56925 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a PRLHR-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the PRLHR-derived synthetic peptide biotin-ado-ado-GQNMTVSVVI, with composite pKd 4.3149219 (sheet row 5941). The sequence crosswalk retains the literal P49683 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a GNG4-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the GNG4-derived synthetic peptide biotin-ado-ado-REKKFFCTIL, with composite pKd 4.3808526 (sheet row 5341). The sequence crosswalk retains the literal P50150 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal PDLIM4 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for PDLIM4 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 45403, 54892, 58587 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal PDLIM4 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for PDLIM4 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 26559, 26560, 26561 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a RAB9A-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the RAB9A-derived synthetic peptide biotin-ado-ado-RKPKPSSSCC, with composite pKd 4.1005002 (sheet row 8211). The sequence crosswalk retains the literal P51151 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal EFNB2 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for EFNB2 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 35161, 42888, 44670 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a MAPK12-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the MAPK12-derived synthetic peptide biotin-ttds-GARVSKETPL, with composite pKd 4.2771503 (sheet row 6300). The sequence crosswalk retains the literal P53778 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal SLC16A1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for SLC16A1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 28248, 28249, 28250 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a EPHB3-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the EPHB3-derived synthetic peptide biotin-ado-ado-QMNQTLPVQV, with composite pKd 3.5581273 (sheet row 16461). The sequence crosswalk retains the literal P54753 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a CLDN8-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CLDN8-derived synthetic peptide biotin-ado-ado-PSVYSRSQYV, with composite pKd 3.7360529 (sheet row 13231). The sequence crosswalk retains the literal P56748 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal CLDN18 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CLDN18 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 57147, 59623, 62782 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal CLDN20 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CLDN20 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 44009, 45753, 49951 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a JAM2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the JAM2-derived synthetic peptide biotin-ado-ado-DFKHTKSFII, with composite pKd 4.1955586 (sheet row 7111). The sequence crosswalk retains the literal P57087 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal CLDN2 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CLDN2 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 40055, 45598, 55003 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a PTEN-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the PTEN-derived synthetic peptide biotin-ttds-DEDQHTQITKacV, with composite pKd 4.5624424 (sheet row 4027). The sequence crosswalk retains the literal P60484 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal DCAF7 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for DCAF7 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 37817, 40187, 51294 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a HNRNPK-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the HNRNPK-derived synthetic peptide biotin-ado-ado-VKQYADVEGF, with composite pKd 4.0930334 (sheet row 8306). The sequence crosswalk retains the literal P61978-2 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal TBPL1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for TBPL1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 36500, 48360, 49044 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a TUBB4B-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the TUBB4B-derived synthetic peptide biotin-ado-ado-FEEEAEEEVA, with composite pKd 4.0104051 (sheet row 9299). The sequence crosswalk retains the literal P68371 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal CLDN10 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CLDN10 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 37362, 51848, 59215 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a JAG1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the JAG1-derived synthetic peptide biotin-ado-ado-QSLNRMEYIV, with composite pKd 4.4478471 (sheet row 4804). The sequence crosswalk retains the literal P78504 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ADAM17-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ADAM17-derived synthetic peptide biotin-ado-ado-NRVDSKETEC, with composite pKd 4.6671172 (sheet row 3377). The sequence crosswalk retains the literal P78536 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal PLCB2 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for PLCB2 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 44524, 46272, 46495 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a CACNA1D-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CACNA1D-derived synthetic peptide biotin-ado-ado-ADEMICITTL, with composite pKd 4.4626127 (sheet row 4691). The sequence crosswalk retains the literal Q01668 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal SLC6A3 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for SLC6A3 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 35605, 54473, 59054 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a APBA1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the APBA1-derived synthetic peptide biotin-ado-ado-LTAQEQPVYI, with composite pKd 4.062852 (sheet row 8654). The sequence crosswalk retains the literal Q02410 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a MUC3A-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the MUC3A-derived synthetic peptide biotin-ado-ado-KRPEMTSSSV, with composite pKd 4.2891382 (sheet row 6197). The sequence crosswalk retains the literal Q02505 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a GHRHR-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GHRHR-derived synthetic peptide biotin-ado-ado-SAAKVLTSMC, with composite pKd 4.1172184 (sheet row 8012). The sequence crosswalk retains the literal Q02643 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a FKBP4-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the FKBP4-derived synthetic peptide biotin-ado-ado-GSQSQVETEA, with composite pKd 4.204983 (sheet row 7013). The sequence crosswalk retains the literal Q02790 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal PTH1R pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for PTH1R are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 48385, 52678, 62345 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a GRIN1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GRIN1-derived synthetic peptide Biotin-Ahx-LSDPSVSTVV, with composite pKd 4.58 (sheet row 3924). The sequence crosswalk retains the literal Q05586-2 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal TYRO3 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for TYRO3 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 39321, 44102, 44668 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal SLC34A1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for SLC34A1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 35892, 45680, 58395 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a CDK18-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CDK18-derived synthetic peptide biotin-ado-ado-RGKNRRQSIF, with composite pKd 4.1916718 (sheet row 7140). The sequence crosswalk retains the literal Q07002 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal VAC14 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for VAC14 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 36430, 37991, 39910 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a KCNA1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the KCNA1-derived synthetic peptide biotin-ado-ado-VNKSKLLTDV, with composite pKd 4.6973956 (sheet row 3193). The sequence crosswalk retains the literal Q09470 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 recognizes the native GluN2A receptor-tail motif.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GRIN2A-derived synthetic peptide biotin-ado-ado-KKMPSIESDV, with composite pKd 5.2480558 (sheet row 1137). The sequence crosswalk retains the literal Q12879 identity. This native receptor motif supports ionotropic glutamate receptor binding in the established DLG3–GluN2 recognition mechanism. It is consistent with the controlled receptor-tail experiment in PMID:10026200 while preserving that experiment's rat peptide and the present human fragment scope. The holdup measurement alone does not demonstrate full-length proteins interacting in cells or receptor regulation.

Proposed replacements: ionotropic glutamate receptor binding

Summary: The literal TRAF2 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for TRAF2 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 35885, 38201, 49952 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a FOXI1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the FOXI1-derived synthetic peptide biotin-ado-ado-VLYPREGTEV, with composite pKd 4.5857796 (sheet row 3891). The sequence crosswalk retains the literal Q12951 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a GRIK2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GRIK2-derived synthetic peptide biotin-ado-ado-RRLPGKETMA, with composite pKd 4.1755023 (sheet row 7332). The sequence crosswalk retains the literal Q13002 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a TIAM1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the TIAM1-derived synthetic peptide Biotin-Ahx-APSRKLNTEI, with composite pKd 3.72 (sheet row 13502). The sequence crosswalk retains the literal Q13009 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a PPFIA1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the PPFIA1-derived synthetic peptide biotin-ado-ado-DSATVRTYSC, with composite pKd 4.0836123 (sheet row 8413). The sequence crosswalk retains the literal Q13136 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 recognizes the native GluN2B receptor-tail motif.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GRIN2B-derived synthetic peptide Biotin-Ahx-EKLSSIESDV, with composite pKd 4.96 (sheet row 1952). The sequence crosswalk retains the literal Q13224 identity. This native receptor motif supports ionotropic glutamate receptor binding in the established DLG3–GluN2 recognition mechanism. It is consistent with the controlled receptor-tail experiment in PMID:10026200 while preserving that experiment's rat peptide and the present human fragment scope. The holdup measurement alone does not demonstrate full-length proteins interacting in cells or receptor regulation.

Proposed replacements: ionotropic glutamate receptor binding

Summary: The literal CTBP1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CTBP1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 43778, 44712, 53030 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal AQP6 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for AQP6 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 36259, 45047, 48516 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a DGKZ-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the DGKZ-derived synthetic peptide biotin-ttds-IQREDQETAV, with composite pKd 4.8825267 (sheet row 2274). The sequence crosswalk retains the literal Q13574 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal ARHGEF7 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for ARHGEF7 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 22752, 22753, 22754 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal RCN2 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for RCN2 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 35344, 43883, 46908 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a FZD2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the FZD2-derived synthetic peptide biotin-ado-ado-TNSRHGETTV, with composite pKd 4.7156569 (sheet row 3077). The sequence crosswalk retains the literal Q14332 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a KCNJ12-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the KCNJ12-derived synthetic peptide biotin-ttds-QRPYRRESEI, with composite pKd 4.3160236 (sheet row 5930). The sequence crosswalk retains the literal Q14500 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a FAT1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the FAT1-derived synthetic peptide biotin-ado-ado-PLDSQQHTEV, with composite pKd 4.7736317 (sheet row 2779). The sequence crosswalk retains the literal Q14517 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SCN5A-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SCN5A-derived synthetic peptide biotin-ado-ado-SPDRDRESIV, with composite pKd 4.5723507 (sheet row 3966). The sequence crosswalk retains the literal Q14524 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal SLC17A1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for SLC17A1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 53760, 60007, 62661 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 recognizes the native GluN2C receptor-tail motif.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GRIN2C-derived synthetic peptide biotin-ado-ado-RRISSLESEV, with composite pKd 5.2683385 (sheet row 1101). The sequence crosswalk retains the literal Q14957 identity. This native receptor motif supports ionotropic glutamate receptor binding in the established DLG3–GluN2 recognition mechanism. It is consistent with the controlled receptor-tail experiment in PMID:10026200 while preserving that experiment's rat peptide and the present human fragment scope. The holdup measurement alone does not demonstrate full-length proteins interacting in cells or receptor regulation.

Proposed replacements: ionotropic glutamate receptor binding

Summary: DLG3 recognizes a motif of the cytoskeletal regulator FRMPD4.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the FRMPD4-derived synthetic peptide biotin-ttds-RLPKIKETTV, with composite pKd 5.6003888 (sheet row 621). The sequence crosswalk retains the literal Q14CM0 identity. PMID:19118189 independently includes SAP102 in Preso/FRMPD4 motif-dependent interactions and rat-brain complexes, and establishes the partner's spine/cytoskeletal regulatory role. This supports cytoskeletal regulatory protein binding without transferring the partner's activity to DLG3 or treating this fragment assay as a full-length physiological complex.

Proposed replacements: cytoskeletal regulatory protein binding

Summary: DLG3 PDZ-domain binding to a KARS1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the KARS1-derived synthetic peptide biotin-ado-ado-LESTTVGTSV, with composite pKd 4.5061158 (sheet row 4391). The sequence crosswalk retains the literal Q15046 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a PLCB4-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the PLCB4-derived synthetic peptide biotin-ttds-EMDRRPATVV, with composite pKd 4.2366873 (sheet row 6678). The sequence crosswalk retains the literal Q15147 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a NECTIN1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the NECTIN1-derived synthetic peptide biotin-ado-ado-SFISKKEWYV, with composite pKd 4.1073706 (sheet row 8122). The sequence crosswalk retains the literal Q15223 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal RCN1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for RCN1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 37274, 58136, 62279 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 recognizes a receptor tyrosine kinase tail.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ERBB4-derived synthetic peptide biotin-ado-ado-PPYRHRNTVV, with composite pKd 4.7896258 (sheet row 2706). The sequence crosswalk retains the literal Q15303 identity. The independent human-brain screen in PMID:10725395 explicitly recovered SAP102 using the ERBB4 cytoplasmic tail, supporting receptor tyrosine kinase binding. That paper's later PSD-95-only assays are not attributed to DLG3, and this holdup result does not imply receptor activation or a native full-length complex.

Proposed replacements: receptor tyrosine kinase binding

Summary: DLG3 PDZ-domain binding to a RALBP1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the RALBP1-derived synthetic peptide biotin-ttds-PSRDRKETSI, with composite pKd 4.7665743 (sheet row 2809). The sequence crosswalk retains the literal Q15311 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a EPHA7-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the EPHA7-derived synthetic peptide biotin-ado-ado-LHLHGTGIQV, with composite pKd 3.5076589 (sheet row 17525). The sequence crosswalk retains the literal Q15375 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a RPS6KA1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the RPS6KA1-derived synthetic peptide Biotin-ttds-RRVRKLPSTpTL , with composite pKd 3.89 (sheet row 10910). The sequence crosswalk retains the literal Q15418 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal NHERF2 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for NHERF2 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 26010, 26011, 26012 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal OR8G1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for OR8G1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 38012, 47117, 47989 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a TRIP6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the TRIP6-derived synthetic peptide biotin-ado-ado-ELSATVTTDC, with composite pKd 4.2288328 (sheet row 6756). The sequence crosswalk retains the literal Q15654 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a CD226-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the CD226-derived synthetic peptide biotin-ado-ado-TFSRRPKTRV, with composite pKd 3.8063262 (sheet row 12157). The sequence crosswalk retains the literal Q15762 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a EFNB3-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the EFNB3-derived synthetic peptide biotin-ado-ado-QSPPNIYYKV, with composite pKd 3.5576035 (sheet row 16467). The sequence crosswalk retains the literal Q15768 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a PKN2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the PKN2-derived synthetic peptide biotin-ado-ado-RDFDYIADWC, with composite pKd 4.1630236 (sheet row 7478). The sequence crosswalk retains the literal Q16513 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a C3AR1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the C3AR1-derived synthetic peptide biotin-ado-ado-VISERNSTTV, with composite pKd 4.420184 (sheet row 5036). The sequence crosswalk retains the literal Q16581 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a DUSP5-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the DUSP5-derived synthetic peptide biotin-ado-ado-RSPVATATSC, with composite pKd 4.181248 (sheet row 7258). The sequence crosswalk retains the literal Q16690 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SLC5A12-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SLC5A12-derived synthetic peptide biotin-ado-ado-NNMAFETTHF, with composite pKd 4.0800089 (sheet row 8458). The sequence crosswalk retains the literal Q1EHB4 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal ACOT6 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for ACOT6 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 42757, 49782, 64967 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a PRR16-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the PRR16-derived synthetic peptide biotin-ado-ado-ILRKSTTTTV, with composite pKd 5.0688082 (sheet row 1612). The sequence crosswalk retains the literal Q569H4 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SDK2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SDK2-derived synthetic peptide biotin-ado-ado-APIAGFSSFV, with composite pKd 4.0691113 (sheet row 8582). The sequence crosswalk retains the literal Q58EX2 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SLC45A4-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SLC45A4-derived synthetic peptide biotin-ado-ado-QGPVETESVV, with composite pKd 4.4746854 (sheet row 4589). The sequence crosswalk retains the literal Q5BKX6 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a XKR7-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the XKR7-derived synthetic peptide biotin-ado-ado-QELLEYETTV, with composite pKd 4.8459453 (sheet row 2439). The sequence crosswalk retains the literal Q5GH72 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal CRB2 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CRB2 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 36636, 39571, 39796 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a ZNF831-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ZNF831-derived synthetic peptide biotin-ado-ado-DDEDRLVIEI, with composite pKd 4.003069 (sheet row 9397). The sequence crosswalk retains the literal Q5JPB2 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a IQSEC2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the IQSEC2-derived synthetic peptide biotin-ado-ado-AKPSRISTVV, with composite pKd 5.331498 (sheet row 979). The sequence crosswalk retains the literal Q5JU85 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal KCNT1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for KCNT1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 43099, 52394, 58625 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal DGKK pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for DGKK are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 30341, 30342, 30343 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a SAPCD1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the SAPCD1-derived synthetic peptide biotin-ado-ado-TKGPRGPTRV, with composite pKd 4.4354975 (sheet row 4920). The sequence crosswalk retains the literal Q5SSQ6 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a FRMPD1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_3 binding to the FRMPD1-derived synthetic peptide Biotin-Ahx-TQKFRASTAL, with composite pKd 3.85 (sheet row 11497). The sequence crosswalk retains the literal Q5SYB0 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal PDZK1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for PDZK1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 26141, 26142, 26143 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a GPRC6A-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GPRC6A-derived synthetic peptide biotin-ado-ado-TLPRKRMSSI, with composite pKd 4.2277578 (sheet row 6773). The sequence crosswalk retains the literal Q5T6X5 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a KLHDC7A-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the KLHDC7A-derived synthetic peptide biotin-ado-ado-PTPDLPQTRV, with composite pKd 3.9959905 (sheet row 9486). The sequence crosswalk retains the literal Q5VTJ3 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ARHGEF16-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ARHGEF16-derived synthetic peptide biotin-ttds-MERLRVETDV, with composite pKd 5.6085949 (sheet row 608). The sequence crosswalk retains the literal Q5VV41 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a TMEM215-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the TMEM215-derived synthetic peptide Biotin-Ahx-QGRWDHETIV, with composite pKd 4.8 (sheet row 2657). The sequence crosswalk retains the literal Q68D42 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: Retain the independently supported ARHGAP17 association.

Reason: Independent BioPlex and primary AP-MS graph evidence supports the ARHGAP17 association despite undetected PDZ-tail binding. These co-complex captures do not independently establish recognition of a cytoskeletal regulator, so retain the supported association without a partner-class MF refinement or an inferred GAP-inhibition mechanism.

Summary: DLG3 PDZ-domain binding to a DENND5A-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the DENND5A-derived synthetic peptide biotin-ado-ado-ETSLVKGIDI, with composite pKd 3.5735929 (sheet row 16116). The sequence crosswalk retains the literal Q6IQ26 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a KCNV1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the KCNV1-derived synthetic peptide biotin-ado-ado-RSSGGDDFWF, with composite pKd 4.0550409 (sheet row 8774). The sequence crosswalk retains the literal Q6PIU1 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a SLC2A7-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the SLC2A7-derived synthetic peptide biotin-ado-ado-TASPAKETSF, with composite pKd 4.2455007 (sheet row 6595). The sequence crosswalk retains the literal Q6PXP3 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a TRAF7-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the TRAF7-derived synthetic peptide biotin-ado-ado-VDSTVKVWTC, with composite pKd 4.1825448 (sheet row 7243). The sequence crosswalk retains the literal Q6Q0C0 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal CSPG4 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for CSPG4 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 35576, 42988, 51374 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a KCNT2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the KCNT2-derived synthetic peptide biotin-ttds-GQDSREETQL, with composite pKd 3.9956189 (sheet row 9493). The sequence crosswalk retains the literal Q6UVM3 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a CES3-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the CES3-derived synthetic peptide biotin-ado-ado-QKNRKAQEDL, with composite pKd 4.2149682 (sheet row 6911). The sequence crosswalk retains the literal Q6UWW8 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal TMIGD1 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for TMIGD1 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 29180, 29181, 29182 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a DCHS2-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the DCHS2-derived synthetic peptide biotin-ado-ado-ELKAEDEVQI, with composite pKd 3.5903082 (sheet row 15783). The sequence crosswalk retains the literal Q6V1P9 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a NPSR1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the NPSR1-derived synthetic peptide biotin-ado-ado-MQILSKPEFI, with composite pKd 4.1829291 (sheet row 7238). The sequence crosswalk retains the literal Q6W5P4 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a PLEKHG7-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the PLEKHG7-derived synthetic peptide biotin-ado-ado-FTLPAESSEI, with composite pKd 4.1913887 (sheet row 7145). The sequence crosswalk retains the literal Q6ZR37 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a RASSF6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the RASSF6-derived synthetic peptide biotin-ttds-KLVIKTETTV, with composite pKd 5.5338154 (sheet row 687). The sequence crosswalk retains the literal Q6ZTQ3 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a GOLT1A-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the GOLT1A-derived synthetic peptide biotin-ado-ado-RRLQGTSSMV, with composite pKd 4.6689086 (sheet row 3365). The sequence crosswalk retains the literal Q6ZVE7 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal RSRC2 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for RSRC2 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 36933, 46221, 56586 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a TRPM1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the TRPM1-derived synthetic peptide biotin-ado-ado-KEKASTETEC, with composite pKd 3.9156229 (sheet row 10553). The sequence crosswalk retains the literal Q7Z4N2 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a NET1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the NET1-derived synthetic peptide biotin-ttds-SGGKRKETLV, with composite pKd 5.4319113 (sheet row 811). The sequence crosswalk retains the literal Q7Z628 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ORF putative E6-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ORF putative E6-derived synthetic peptide biotin-ttds-QRQARSETLV, with composite pKd 5.1716783 (sheet row 1325). The sequence crosswalk retains the literal Q81964 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ADGRA1-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ADGRA1-derived synthetic peptide biotin-ado-ado-TGPWKNETTV, with composite pKd 5.0096233 (sheet row 1796). The sequence crosswalk retains the literal Q86SQ6 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal MYPN pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for MYPN are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 37247, 42744, 45711 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a MARCHF3-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the MARCHF3-derived synthetic peptide biotin-ado-ado-VKRNSKETVV, with composite pKd 5.5196186 (sheet row 701). The sequence crosswalk retains the literal Q86UD3 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: DLG3 PDZ-domain binding to a ZSCAN30-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the ZSCAN30-derived synthetic peptide biotin-ado-ado-MQHQRTHTRV, with composite pKd 4.8843263 (sheet row 2267). The sequence crosswalk retains the literal Q86W11 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal UNC93A pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for UNC93A are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 41769, 42642, 44073 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: The literal DGKH pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for DGKH are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 57391, 63430, 64923 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a RNF130-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the RNF130-derived synthetic peptide biotin-ado-ado-SLNANEVEWF, with composite pKd 4.2201743 (sheet row 6859). The sequence crosswalk retains the literal Q86XS8 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal TRIM50 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for TRIM50 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 39257, 40694, 45822 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a MARCHF9-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the MARCHF9-derived synthetic peptide biotin-ado-ado-REVVMRVTTV, with composite pKd 5.2348157 (sheet row 1166). The sequence crosswalk retains the literal Q86YJ5 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.

Summary: The literal PLEKHH2 pair remains unresolved at the measured scope.

Reason: All mapped SD1 composite values for PLEKHH2 are zero, and no above-threshold alternative assay or independently established pair was found in the bounded source audit. The actual paper explicitly distinguishes below-threshold measurements from biological non-interactions. SD1 sheet rows 43965, 56367, 60812 and the exact IntAct crosswalk were checked; negative=false and the encoded 1.0x10(molar) value are not treated as positive affinity evidence. Keep this literal pair unresolved, without REMOVE or a claim that DLG3 cannot bind proteins generally.

Summary: DLG3 PDZ-domain binding to a FMNL3-derived peptide is retained as a non-core association.

Reason: The original SD1 PDZ-PBM-interactome sheet reports DLG3_2 binding to the FMNL3-derived synthetic peptide biotin-ado-ado-DAAHHDESNC, with composite pKd 4.0931945 (sheet row 8303). The sequence crosswalk retains the literal Q8IVF7 identity. Retain this positive domain–motif association as non-core. The synthetic ligand experiment does not establish a native full-length interaction or a more specific biological role; a generic peptide-binding replacement would restate the assay format.