FRMPD4 (Preso/Preso1) is a multidomain neuronal scaffold containing WW, PDZ and FERM domains and a C-terminal PDZ-binding motif. Its C-terminal motif binds PSD-95-family and other PDZ domains, while its FERM region binds phosphatidylinositol-4,5-bisphosphate, linking protein interactions to membrane and dendritic-spine localization. Human FRMPD4 constructs regulate spine density in rodent neurons, and human loss-of-function variants are associated with X-linked intellectual disability. Separate rat and mouse studies connect Preso1 to Homerβmetabotropic glutamate receptor organization and regulation of receptor phosphorylation. Binding of purified fragments defines additional molecular contacts but does not by itself establish their endogenous physiological roles.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:19118189 Preso, a novel PSD-95-interacting FERM and PDZ domain protei... | MODIFY | Summary: Refine the demonstrated DLG4/PSD-95 interaction to PDZ domain binding. Reason: PMID:19118189 assays human Preso/FRMPD4 and its terminal motif against PSD-95-family proteins, including the exact original partner P78352 (DLG4/PSD-95). Yeast two-hybrid, pull-down and heterologous co-immunoprecipitation, together with C-terminal deletion/mutation, identify the target motif binding partner PDZ domains. This is positive, oriented support for GO:0030165, a more informative molecular function than generic protein binding. Rat brain recovery and neuronal phenotypes are distinct evidence contexts; they do not establish every human endogenous complex or a function unique to a natural isoform. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19118189 Preso, a novel PSD-95-interacting FERM and PDZ domain protei... | MODIFY | Summary: Refine the demonstrated DLG1/SAP97 interaction to PDZ domain binding. Reason: PMID:19118189 assays human Preso/FRMPD4 and its terminal motif against PSD-95-family proteins, including the exact original partner Q12959 (DLG1/SAP97). Yeast two-hybrid, pull-down and heterologous co-immunoprecipitation, together with C-terminal deletion/mutation, identify the target motif binding partner PDZ domains. This is positive, oriented support for GO:0030165, a more informative molecular function than generic protein binding. Rat brain recovery and neuronal phenotypes are distinct evidence contexts; they do not establish every human endogenous complex or a function unique to a natural isoform. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19118189 Preso, a novel PSD-95-interacting FERM and PDZ domain protei... | KEEP AS NON CORE | Summary: Retain the ARHGEF7/Ξ²Pix association without assigning its exchange activity to FRMPD4. Reason: The exact Q14155 partner is Ξ²Pix/ARHGEF7. PMID:19118189 reports cellular co-immunoprecipitation and loss of binding with the FRMPD4 PDZ-site R102A mutant. This supports a scaffold-associated interaction, while Ξ²Pix performs guanine-nucleotide exchange. The experiment does not show FRMPD4 binding a partner PDZ domain, nor a new FRMPD4 catalytic activity. Retain this positive association as non-core; preserve its original partner and source. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19118189 Preso, a novel PSD-95-interacting FERM and PDZ domain protei... | MODIFY | Summary: Refine the demonstrated DLG2/PSD-93 interaction to PDZ domain binding. Reason: PMID:19118189 assays human Preso/FRMPD4 and its terminal motif against PSD-95-family proteins, including the exact original partner Q15700 (DLG2/PSD-93). Yeast two-hybrid, pull-down and heterologous co-immunoprecipitation, together with C-terminal deletion/mutation, identify the target motif binding partner PDZ domains. This is positive, oriented support for GO:0030165, a more informative molecular function than generic protein binding. Rat brain recovery and neuronal phenotypes are distinct evidence contexts; they do not establish every human endogenous complex or a function unique to a natural isoform. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19118189 Preso, a novel PSD-95-interacting FERM and PDZ domain protei... | MODIFY | Summary: Refine the demonstrated DLG3/SAP102 interaction to PDZ domain binding. Reason: PMID:19118189 assays human Preso/FRMPD4 and its terminal motif against PSD-95-family proteins, including the exact original partner Q92796 (DLG3/SAP102). Yeast two-hybrid, pull-down and heterologous co-immunoprecipitation, together with C-terminal deletion/mutation, identify the target motif binding partner PDZ domains. This is positive, oriented support for GO:0030165, a more informative molecular function than generic protein binding. Rat brain recovery and neuronal phenotypes are distinct evidence contexts; they do not establish every human endogenous complex or a function unique to a natural isoform. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22074847 Structural basis for interaction between the conserved cell ... | MODIFY | Summary: Refine the human FRMPD4βGPSM2 interaction to TPR domain binding. Reason: PMID:22074847 identifies binding between FRMPD4 residues 978β1025 and the LGN/GPSM2 TPR region (13β414), including competition with mInsc in the selected main-article assays. The 2011 crystal structure concerns mInscβLGN, so it is not a FRMPD4 structure. Independent PMID:25664792 explicitly tests the human FRMPD4 segment, resolves its LGN complex at 1.5 Γ
and tests interface substitutions. These support the exact P81274 association, without transferring mInsc spindle-orientation physiology or interpreting the bound LGN TPR as a PDZ domain. GO:0030911 specifically describes binding to a tetratricopeptide-repeat domain and therefore captures the measured interface more precisely than generic protein binding. Proposed replacements: TPR domain binding |
| GO:0005515 protein binding | IPI PMID:24550280 Large-scale interaction profiling of PDZ domains through pro... | MODIFY | Summary: Refine the verified human FRMPD4 peptideβDLG1 PDZ2 interaction. Reason: The original PMID:24550280 Supporting Information Table S1 lists FRPD4_HUMAN peptide KIKETTV with DLG1 PDZ2 and 15/12 replicate reads (27 total). The Methods use a human C-terminal peptide library on M13 phage and purified GST-PDZ bait. This directly identifies the orientation required for PDZ domain binding. It verifies the original Q12959 pair despite its absence from the current target IntAct response. Selection enrichment is not a full-length endogenous co-complex or an affinity measurement. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:29267967 FRMPD4 mutations cause X-linked intellectual disability and ... | KEEP AS NON CORE | Summary: Retain the human FRMPD4βmouse Homer1c association with its exact tested partner. Reason: PMID:29267967 compares tagged human wild-type FRMPD4 with the p.Cys618Valfs*8 construct in HEK293T co-immunoprecipitation assays with HA-Homer1c; the truncated construct loses association. The original GOA partner Q9Z214-1 is mouse Homer1c and remains unchanged. The selected Methods do not independently establish that clone sequence, and the heterologous association does not prove direct binary affinity. Auxiliary PMID:22561452 provides a rat Preso1/Homer anchoring mechanism and mouse physiology; it does not convert this source into an endogenous human or human-Homer assay. |
| GO:0005515 protein binding | IPI PMID:30126976 Proteome-wide analysis of phospho-regulated PDZ domain inter... | MODIFY | Summary: Refine the FRMPD4 C-terminal peptide interaction with P78352/DLG4 to PDZ domain binding. Reason: PMID:30126976 uses human C-terminal nine-residue peptides in phage-display selections against PDZ domains. The exact original partner P78352/DLG4, PDZ region 313β388, is represented with FRMPD4 residues 1314β1322 in the retained IntAct record(s). Original Figure5A was independently viewed: the WT LPKIKETTV red bar is positive in the DLG4 PDZ3 panel, with the T1320E blue bar lower. No numerical value is extracted from the image. This is the target peptide binding the partner PDZ domain, not merely the presence of a PDZ domain in either protein. WT selections support GO:0030165; the T1320E library comparison is a phosphomimetic experiment, not proof of endogenous FRMPD4 phosphorylation or a cellular kinase mechanism. No full-length physiological interaction is inferred. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30126976 Proteome-wide analysis of phospho-regulated PDZ domain inter... | MODIFY | Summary: Refine the FRMPD4 C-terminal peptide interaction with Q12959/DLG1 to PDZ domain binding. Reason: PMID:30126976 uses human C-terminal nine-residue peptides in phage-display selections against PDZ domains. The exact original partner Q12959/DLG1, PDZ1, PDZ2 and PDZ3, is represented with FRMPD4 residues 1314β1322 in the retained IntAct record(s). Original Table EV3 contains WT FRMPD4 rows124/159/187 for these domains. This is the target peptide binding the partner PDZ domain, not merely the presence of a PDZ domain in either protein. WT selections support GO:0030165; the T1320E library comparison is a phosphomimetic experiment, not proof of endogenous FRMPD4 phosphorylation or a cellular kinase mechanism. No full-length physiological interaction is inferred. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30126976 Proteome-wide analysis of phospho-regulated PDZ domain inter... | MODIFY | Summary: Refine the FRMPD4 C-terminal peptide interaction with Q13424/SNTA1 to PDZ domain binding. Reason: PMID:30126976 uses human C-terminal nine-residue peptides in phage-display selections against PDZ domains. The exact original partner Q13424/SNTA1, PDZ region 87β166, is represented with FRMPD4 residues 1314β1322 in the retained IntAct record(s). Original Figure5A was independently viewed: the WT LPKIKETTV red bar is positive in the SNTA1 PDZ panel, with the T1320E blue bar lower. No numerical value is extracted from the image. This is the target peptide binding the partner PDZ domain, not merely the presence of a PDZ domain in either protein. WT selections support GO:0030165; the T1320E library comparison is a phosphomimetic experiment, not proof of endogenous FRMPD4 phosphorylation or a cellular kinase mechanism. No full-length physiological interaction is inferred. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30126976 Proteome-wide analysis of phospho-regulated PDZ domain inter... | MODIFY | Summary: Refine the FRMPD4 C-terminal peptide interaction with Q13884/SNTB1 to PDZ domain binding. Reason: PMID:30126976 uses human C-terminal nine-residue peptides in phage-display selections against PDZ domains. The exact original partner Q13884/SNTB1, PDZ region 112β191, is represented with FRMPD4 residues 1314β1322 in the retained IntAct record(s). Original Figure5A was independently viewed: the WT LPKIKETTV red bar is positive in the SNTB1 PDZ panel, with the T1320E blue bar lower. No numerical value is extracted from the image. This is the target peptide binding the partner PDZ domain, not merely the presence of a PDZ domain in either protein. WT selections support GO:0030165; the T1320E library comparison is a phosphomimetic experiment, not proof of endogenous FRMPD4 phosphorylation or a cellular kinase mechanism. No full-length physiological interaction is inferred. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30126976 Proteome-wide analysis of phospho-regulated PDZ domain inter... | MODIFY | Summary: Refine the FRMPD4 C-terminal peptide interaction with Q14160/SCRIB to PDZ domain binding. Reason: PMID:30126976 uses human C-terminal nine-residue peptides in phage-display selections against PDZ domains. The exact original partner Q14160/SCRIB, PDZ1 and PDZ3, is represented with FRMPD4 residues 1314β1322 in the retained IntAct record(s). Original Table EV3 contains WT FRMPD4 rows23/79 for these domains. This is the target peptide binding the partner PDZ domain, not merely the presence of a PDZ domain in either protein. WT selections support GO:0030165; the T1320E library comparison is a phosphomimetic experiment, not proof of endogenous FRMPD4 phosphorylation or a cellular kinase mechanism. No full-length physiological interaction is inferred. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30126976 Proteome-wide analysis of phospho-regulated PDZ domain inter... | MODIFY | Summary: Refine the FRMPD4 C-terminal peptide interaction with Q92796/DLG3 to PDZ domain binding. Reason: PMID:30126976 uses human C-terminal nine-residue peptides in phage-display selections against PDZ domains. The exact original partner Q92796/DLG3, PDZ region 226β309, is represented with FRMPD4 residues 1314β1322 in the retained IntAct record(s). Original Figure5A was independently viewed: the WT LPKIKETTV red bar is positive in the DLG3 PDZ2 panel, with the T1320E blue bar lower. No numerical value is extracted from the image. This is the target peptide binding the partner PDZ domain, not merely the presence of a PDZ domain in either protein. WT selections support GO:0030165; the T1320E library comparison is a phosphomimetic experiment, not proof of endogenous FRMPD4 phosphorylation or a cellular kinase mechanism. No full-length physiological interaction is inferred. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33864728 Host PDZ-containing proteins targeted by SARS-CoV-2. | KEEP AS NON CORE | Summary: Retain measured FRMPD4 PDZ binding to the MERS coronavirus E peptide. Reason: Although PMID:33864728 foregrounds SARS-CoV-2, its original Table 1 explicitly contains the MERS EβFRMPD4 result: binding intensity 0.31 and estimated Kd 43 Β΅M. The original K9N5R3 partner is the MERS coronavirus E protein; the assay uses its C-terminal peptide and human FRMPD4 PDZ residues 67β160. The in-vitro holdup measurement supports binding. It does not establish human infection participation, and the orientation does not demonstrate FRMPD4 binding a partner PDZ domain. Separate SARS-CoV-2 and infection-perturbation results are not substituted for this exact interaction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: Retain quantified binding of FRMPD4βs own PDZ domain to K9N5R3. Reason: PMID:36115835 Supplementary Dataset 1 positively quantifies human FRMPD4 PDZ residues 67β160 binding the partner C-terminal motif: row 8525: partner motif MERS-E, composite pKd 4.07428006. This supports the exact original K9N5R3 protein-binding assertion. It does not show FRMPD4 binding a PDZ domain on that partner; therefore GO:0030165 would reverse the demonstrated orientation here. The peptide/domain assay is retained as non-core and does not establish a full-length endogenous complex or an infection, junctional or sensory process. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact O00560 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner O00560, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact O14745 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner O14745, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβO14924 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 3720: RGS12, composite pKd 4.61120032. This supports PDZ domain binding rather than generic protein binding for the original O14924 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβO15018 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 8819: PDZD2_2, composite pKd 4.05090601. This supports PDZ domain binding rather than generic protein binding for the original O15018 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact O60759 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner O60759, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact O75970 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner O75970, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: Retain quantified binding of FRMPD4βs own PDZ domain to O95049. Reason: PMID:36115835 Supplementary Dataset 1 positively quantifies human FRMPD4 PDZ residues 67β160 binding the partner C-terminal motif: row 11802: partner motif TJP3, composite pKd 3.83. This supports the exact original O95049 protein-binding assertion. It does not show FRMPD4 binding a PDZ domain on that partner; therefore GO:0030165 would reverse the demonstrated orientation here. The positive original TJP3 row is additional author-data support beyond the finite-parameter coverage of the exact IntAct records; their numeric placeholder is not promoted to positive evidence. The peptide/domain assay is retained as non-core and does not establish a full-length endogenous complex or an infection, junctional or sensory process. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβO96018 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 4622: APBA3_2, composite pKd 4.47096977. This supports PDZ domain binding rather than generic protein binding for the original O96018 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact P60484 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner P60484, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβP78352 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 221: DLG4_3, composite pKd 5.25131075; row 622: DLG4_2, composite pKd 5.59916477; row 1680: DLG4_1, composite pKd 5.04871461. This supports PDZ domain binding rather than generic protein binding for the original P78352 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q02410 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q02410, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q07157 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q07157, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ12923 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 5986: PTPN13_2, composite pKd 4.31078007. This supports PDZ domain binding rather than generic protein binding for the original Q12923 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ12959 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 421: DLG1_2, composite pKd 6.05645085; row 1040: DLG1_3, composite pKd 5.29609785; row 1443: DLG1_1, composite pKd 5.12374248. This supports PDZ domain binding rather than generic protein binding for the original Q12959 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q13009 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q13009, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ13424 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 398: SNTA1, composite pKd 6.65565615. This supports PDZ domain binding rather than generic protein binding for the original Q13424 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ13884 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 1328: SNTB1, composite pKd 5.17036635. This supports PDZ domain binding rather than generic protein binding for the original Q13884 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ14005 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 8539: IL16_1, composite pKd 4.07305931. This supports PDZ domain binding rather than generic protein binding for the original Q14005 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ14160 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 182: SCRIB_1, composite pKd 4.94753193; row 2308: SCRIB_3, composite pKd 4.87509646; row 2387: SCRIB_4, composite pKd 4.85490938; row 3722: SCRIB_2, composite pKd 4.61106709. This supports PDZ domain binding rather than generic protein binding for the original Q14160 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q15599 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q15599, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ15700 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 739: DLG2_2, composite pKd 5.49515926; row 1004: DLG2_1, composite pKd 5.31864835; row 1373: DLG2_3, composite pKd 5.15094299. This supports PDZ domain binding rather than generic protein binding for the original Q15700 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q5T2W1 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q5T2W1, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ5TCQ9 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 1106: MAGI3_2, composite pKd 5.26596754. This supports PDZ domain binding rather than generic protein binding for the original Q5TCQ9 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q68DX3 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q68DX3, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ6P0Q8 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 170: MAST2, composite pKd 4.93031427. This supports PDZ domain binding rather than generic protein binding for the original Q6P0Q8 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ6ZMN7 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 152: PDZRN4_1, composite pKd 4.66700635; row 4927: PDZRN4_2, composite pKd 4.4345773. This supports PDZ domain binding rather than generic protein binding for the original Q6ZMN7 context. The finite curated affinity values also reconcile numerically to original measurements. The paper separately quantifies the reverse orientation; that does not replace the forward evidence used for this refinement. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ70Z35 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 6504: PREX2_2, composite pKd 4.25443193. This supports PDZ domain binding rather than generic protein binding for the original Q70Z35 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ86UL8 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 222: MAGI2_2, composite pKd 4.73274203; row 6649: MAGI2_4, composite pKd 4.24000711; row 8884: MAGI2_3, composite pKd 4.04585163; row 9705: MAGI2_6, composite pKd 3.9793001; row 10724: MAGI2_5, composite pKd 3.90421125. This supports PDZ domain binding rather than generic protein binding for the original Q86UL8 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q86UT5 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q86UT5, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. The original GOA partner remains canonical Q86UT5; the retained curated feature context specifically includes Q86UT5-2 and is not erased. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ8N448 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 4600: LNX2_2, composite pKd 4.47285711. This supports PDZ domain binding rather than generic protein binding for the original Q8N448 context. The finite curated affinity values also reconcile numerically to original measurements. Blank composite entries for additional domains remain missing values, not zero or evidence of absence. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ8NI35 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 9742: Inadl_8, composite pKd 3.97671151; row 18208: Inadl_9, composite pKd 3.47716671. This supports PDZ domain binding rather than generic protein binding for the original Q8NI35 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ8TBB1 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 18376: LNX1_2, composite pKd 3.42463892. This supports PDZ domain binding rather than generic protein binding for the original Q8TBB1 context. The positive original-paper row(s) extend beyond the exact finite-parameter coverage of the retained curated records; support comes from the matched author data, not from interpreting their 10-M-looking field as positive. The paper separately quantifies the reverse orientation; that does not replace the forward evidence used for this refinement. Blank composite entries for additional domains remain missing values, not zero or evidence of absence. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ8TDM6 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 3190: DLG5_2, composite pKd 4.69801724. This supports PDZ domain binding rather than generic protein binding for the original Q8TDM6 context. The finite curated affinity values also reconcile numerically to original measurements. Blank composite entries for additional domains remain missing values, not zero or evidence of absence. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q8TEU7 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q8TEU7, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q8TEW0 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q8TEW0, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ8TEW8 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 18358: PARD3B_1, composite pKd 3.45326346. This supports PDZ domain binding rather than generic protein binding for the original Q8TEW8 context. The positive original-paper row(s) extend beyond the exact finite-parameter coverage of the retained curated records; support comes from the matched author data, not from interpreting their 10-M-looking field as positive. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q8TF72 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q8TF72, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q92614 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q92614, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ92796 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 621: DLG3_2, composite pKd 5.60038876; row 1231: DLG3_3, composite pKd 5.21086631; row 4335: DLG3_1, composite pKd 4.51318875. This supports PDZ domain binding rather than generic protein binding for the original Q92796 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q96FS4 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q96FS4, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q96JY6 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q96JY6, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ96QZ7 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 2561: MAGI1_3, composite pKd 4.82021721; row 3956: MAGI1_6, composite pKd 4.57467733; row 4447: MAGI1_5, composite pKd 4.49592448; row 4453: MAGI1_2, composite pKd 4.49478112. This supports PDZ domain binding rather than generic protein binding for the original Q96QZ7 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q99767 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q99767, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ9C0E4 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 18390: GRIP2_6, composite pKd 3.39175869. This supports PDZ domain binding rather than generic protein binding for the original Q9C0E4 context. The positive original-paper row(s) extend beyond the exact finite-parameter coverage of the retained curated records; support comes from the matched author data, not from interpreting their 10-M-looking field as positive. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q9H190 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q9H190, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ9H5P4 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 1780: PDZD7_3, composite pKd 5.01417147. This supports PDZ domain binding rather than generic protein binding for the original Q9H5P4 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ9P202 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 7945: DFNB31_2, composite pKd 4.12316099; row 9955: DFNB31_1, composite pKd 3.96180212. This supports PDZ domain binding rather than generic protein binding for the original Q9P202 context. The finite curated affinity values also reconcile numerically to original measurements. The paper separately quantifies the reverse orientation; that does not replace the forward evidence used for this refinement. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: Retain quantified binding of FRMPD4βs own PDZ domain to Q9UDY2. Reason: PMID:36115835 Supplementary Dataset 1 positively quantifies human FRMPD4 PDZ residues 67β160 binding the partner C-terminal motif: row 5579: partner motif TJP2, composite pKd 4.35435608. This supports the exact original Q9UDY2 protein-binding assertion. It does not show FRMPD4 binding a PDZ domain on that partner; therefore GO:0030165 would reverse the demonstrated orientation here. The peptide/domain assay is retained as non-core and does not establish a full-length endogenous complex or an infection, junctional or sensory process. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q9ULL8 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q9ULL8, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Refine the verified FRMPD4 C-terminal motifβQ9UPQ7 PDZ interaction. Reason: Original Supplementary Dataset 1 of PMID:36115835 has positive oriented measurements with FRMPD4βs human C-terminal peptide RLPKIKETTV (1313β1322) binding the partner PDZ domain(s): row 4602: PDZRN3_1, composite pKd 4.47277383. This supports PDZ domain binding rather than generic protein binding for the original Q9UPQ7 context. The finite curated affinity values also reconcile numerically to original measurements. The holdup-derived fragment affinities do not establish an endogenous full-length complex, tissue-specific role, partner catalytic activity, or a core physiological function for each pair. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The exact Q9Y3R0 interaction remains quantitatively unverified in this source. Reason: For the original PMID:36115835 partner Q9Y3R0, every matched author composite affinity is zero and the recorded underlying binding intensities fall below the paperβs applicable assay thresholds. The exact IntAct records carry the 10-M-looking kd:1.0x10(molar) value despite negative=false; its import semantics are unresolved and it is not treated as a measured positive affinity. Thus the current exact source reconciliation cannot verify this specific interaction. Preserve the curator assertion, partner, source and all raw records as UNDECIDED, without asserting absence, a wrong gene, or removal. Positive measurements for other partners cannot validate this context. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: Retain quantified binding of FRMPD4βs own PDZ domain to Q9Y6N9. Reason: PMID:36115835 Supplementary Dataset 1 positively quantifies human FRMPD4 PDZ residues 67β160 binding the partner C-terminal motif: row 5045: partner motif USH1C, composite pKd 4.42. This supports the exact original Q9Y6N9 protein-binding assertion. It does not show FRMPD4 binding a PDZ domain on that partner; therefore GO:0030165 would reverse the demonstrated orientation here. The peptide/domain assay is retained as non-core and does not establish a full-length endogenous complex or an infection, junctional or sensory process. |
| GO:0005546 phosphatidylinositol-4,5-bisphosphate binding | IBA GO_REF:0000033 | ACCEPT | Summary: Retain phylogenetically supported phosphatidylinositol-4,5-bisphosphate binding. Reason: The actual PTHR46221 tree/MSA places the exact human 1322-residue Q14CM0 leaf AN143/PTN002551300 below the incoming IBD node AN135/PTN008705583. Its literal GO:0005546 IBD uses the experimental human Q14CM0 donor from PMID:19118189; self-donation is valid descendant evidence. The human FERM-domain lipid assay independently establishes PIP2 binding. The dated PANTHER19 source and off-target sequence anomalies are disclosed separately and do not alter the exact human path. Supporting Evidence: |
| GO:0005546 phosphatidylinositol-4,5-bisphosphate binding | IDA PMID:19118189 Preso, a novel PSD-95-interacting FERM and PDZ domain protei... | ACCEPT | Summary: Retain direct PIP2 binding by the human FRMPD4 FERM region. Reason: PMID:19118189 tests the human GST-FERM fragment (173β437) with phosphatidylinositol-4,5-bisphosphate-containing liposomes, including competition by neomycin. This supports PIP2 binding as a molecular component of membrane/spine targeting. It does not imply phosphoinositide synthesis, hydrolysis or calcium binding. The negative purified WWβF-actin result in the same paper is a distinct assay and is not converted into direct actin-binding activity. Supporting Evidence: |
| GO:0032991 protein-containing complex | IDA PMID:22074847 Structural basis for interaction between the conserved cell ... | KEEP AS NON CORE | Summary: Retain the experimentally resolved FRMPD4βGPSM2 fragment complex as non-core. Reason: PMID:25664792 resolves a heterodimer of the human FRMPD4 segment and the GPSM2/LGN TPR region, with complementary ITC and interface-substitution assays. Protein-containing complex is an accurate component description for this measured fragment assembly and is as specific as the present annotation vocabulary and evidence establish. Keep it non-core because the experiments do not establish a particular full-length endogenous complex, cellular stoichiometry or a FRMPD4 spindle-orientation role. These are limits on physiological interpretation, not reasons to reject the observed complex. |
| GO:0043197 dendritic spine | IBA GO_REF:0000033 | ACCEPT | Summary: Retain the exact phylogenetic assertion of activity in dendritic spines. Reason: The literal GO:0043197 IBD at PTN008705583/AN135 descends to the verified human AN143 leaf; the experimental human Q14CM0 donor is expected and is not circular. PMID:19118189 connects human FRMPD4 targeting and mutant-dependent function to dendritic spines in rat neuronal cultures. Preserve the original is_active_in relation and the complete donor grouping; this relation is not silently rewritten as the located_in qualifier used by other rows. Supporting Evidence: |
| GO:0043197 dendritic spine | IDA PMID:19118189 Preso, a novel PSD-95-interacting FERM and PDZ domain protei... | ACCEPT | Summary: Retain the experimentally supported dendritic-spine localization. Reason: PMID:19118189 localizes expressed human FRMPD4 at dendritic spines in rat hippocampal neuronal cultures, with targeting defects after domain/motif perturbations; rodent brain localization and biochemical fractions provide separate context. This supports the original IDA localization while preserving the human construct and rodent host distinction. Large rodent immunoreactive bands are not assumed to be separately documented natural human products. Supporting Evidence: |
| GO:0043197 dendritic spine | IEA GO_REF:0000044 | ACCEPT | Summary: Retain the independently supported dendritic-spine localization. Reason: The UniProt SL-0284 electronic localization agrees with the original human FRMPD4 construct localization in cultured neurons and the rodent tissue findings in PMID:19118189. Targeting depends on its terminal PSD-95 interaction, FERM and PDZ modules. Retain the original located_in relation and electronic provenance; do not turn the transfer into an unperformed endogenous human-brain localization assay. Supporting Evidence: |
| GO:0051835 positive regulation of synapse structural plasticity | IMP PMID:19118189 Preso, a novel PSD-95-interacting FERM and PDZ domain protei... | ACCEPT | Summary: Retain positive regulation of dendritic-spine structural plasticity with its tested neuronal scope. Reason: PMID:19118189 introduces human FRMPD4 into embryonic rat hippocampal neurons and measures increased spine density; rat Preso knockdown reduces density and human FRMPD4 rescues it. The PDZ, FERM and terminal targeting modules are required in the tested constructs. These are direct scaffold perturbations supporting the existing structural-plasticity process, with the human construct/rat host distinction explicit. Spine width/length and miniature-current amplitude are separate endpoints; overexpression is not generalized to increased synaptic transmission or endogenous human necessity. Supporting Evidence: |
| GO:0098794 postsynapse | IEA GO_REF:0000117 | TOO GENERAL | Summary: The retained dendritic-spine term supplies the more specific postsynaptic location. Reason: The original ARBA postsynapse inference is biologically compatible with the demonstrated neuronal localization. Official is_a-only ancestry places retained GO:0043197 dendritic spine under GO:0098794 postsynapse, so the accepted narrower location already entails this broad assertion. Mark it TOO_GENERAL on that verified hierarchy, without rejecting its electronic source or erasing the original qualifier. Supporting Evidence: |
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Download this section (compressed HTML)Q: Which domainβmotif interactions measured with purified fragments assemble into endogenous FRMPD4 complexes in human neurons, and which are restricted by localization, abundance or competing partners?
Q: How do the PIP2-binding FERM region, internal PDZ module and C-terminal PDZ-binding motif cooperate to control spine targeting and structural plasticity?
Q: How does endogenous human FRMPD4 organize Homer and metabotropic glutamate receptor signaling, and how closely does that mechanism follow the rat and mouse Preso1 experiments?
Q: For pathogenic truncations, how much of the neuronal phenotype reflects loss of transcript or protein versus effects of a stable truncated product?
Experiment: Use endogenous tagging and reciprocal complex recovery in human neuronal models to test selected contacts with domain-specific rescue constructs; measure spine localization and density alongside protein abundance.
Experiment: Perturb the lipid-binding region and terminal PDZ-binding motif separately and together, with controlled expression and membrane-localization measurements, to separate independent and cooperative contributions.
Experiment: Measure endogenous FRMPD4, Homer and receptor association together with receptor phosphorylation in human neurons, using kinase and binding-site controls; do not infer that FRMPD4 catalyzes phosphorylation.
Experiment: Compare patient-derived transcript stability and endogenous protein abundance with sequence-verified rescue in neuronal models before interpreting overexpressed truncation phenotypes.
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