FKBP52 is an HSP90-associated immunophilin with peptidyl-prolyl isomerase and steroid-receptor co-chaperone functions. It supports androgen receptor transcription in selected reproductive tissues without being required for androgen binding or nuclear import in the examined mouse knockout models. It also participates in glucocorticoid receptor complex trafficking and can regulate Tau-associated microtubule dynamics.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003755 peptidyl-prolyl cis-trans isomerase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Peptidyl-prolyl isomerase activity is an intrinsic FKBP-domain function; it is distinct from HSP90 binding and from the downstream transcriptional consequences of receptor co-chaperoning. Reason: Peptidyl-prolyl isomerase activity is an intrinsic FKBP-domain function; it is distinct from HSP90 binding and from the downstream transcriptional consequences of receptor co-chaperoning. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0003755 peptidyl-prolyl cis-trans isomerase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Peptidyl-prolyl isomerase activity is an intrinsic FKBP-domain function; it is distinct from HSP90 binding and from the downstream transcriptional consequences of receptor co-chaperoning. Reason: Peptidyl-prolyl isomerase activity is an intrinsic FKBP-domain function; it is distinct from HSP90 binding and from the downstream transcriptional consequences of receptor co-chaperoning. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0003755 peptidyl-prolyl cis-trans isomerase activity | ISO GO_REF:0000119 | ACCEPT | Summary: Peptidyl-prolyl isomerase activity is an intrinsic FKBP-domain function; it is distinct from HSP90 binding and from the downstream transcriptional consequences of receptor co-chaperoning. Reason: Peptidyl-prolyl isomerase activity is an intrinsic FKBP-domain function; it is distinct from HSP90 binding and from the downstream transcriptional consequences of receptor co-chaperoning. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0003755 peptidyl-prolyl cis-trans isomerase activity | ISS GO_REF:0000024 | ACCEPT | Summary: Peptidyl-prolyl isomerase activity is an intrinsic FKBP-domain function; it is distinct from HSP90 binding and from the downstream transcriptional consequences of receptor co-chaperoning. Reason: Peptidyl-prolyl isomerase activity is an intrinsic FKBP-domain function; it is distinct from HSP90 binding and from the downstream transcriptional consequences of receptor co-chaperoning. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0005515 protein binding | IPI PMID:11751894 A new first step in activation of steroid receptors: hormone... | REMOVE | Summary: The steroid-receptor-complex interaction is credible, but bare protein binding does not describe the co-chaperone mechanism. Reason: The steroid-receptor-complex interaction is credible, but bare protein binding does not describe the co-chaperone mechanism. Removing this generic label does not dispute the reported interaction. Supporting Evidence: |
| GO:0005524 ATP binding | IDA PMID:8341706 Overexpression, characterization, and purification of a reco... | KEEP AS NON CORE | Summary: The original purified recombinant mouse protein study explicitly reports ATP/GTP binding. Reason: The original purified recombinant mouse protein study explicitly reports ATP/GTP binding. Retain this biochemical observation as peripheral; it neither makes FKBP52 an ATPase/GTPase nor identifies nucleotide hydrolysis as its receptor co-chaperone mechanism. Supporting Evidence: PMID:8341706 The rFKBP-52 possesses an ATP/GTP binding activity that is stimulated by divalent cations. |
| GO:0005525 GTP binding | IDA PMID:8341706 Overexpression, characterization, and purification of a reco... | KEEP AS NON CORE | Summary: The original purified recombinant mouse protein study explicitly reports ATP/GTP binding. Reason: The original purified recombinant mouse protein study explicitly reports ATP/GTP binding. Retain this biochemical observation as peripheral; it neither makes FKBP52 an ATPase/GTPase nor identifies nucleotide hydrolysis as its receptor co-chaperone mechanism. Supporting Evidence: PMID:8341706 The rFKBP-52 possesses an ATP/GTP binding activity that is stimulated by divalent cations. |
| GO:0005634 nucleus | EXP PMID:11751894 A new first step in activation of steroid receptors: hormone... | ACCEPT | Summary: The curated receptor-complex studies support nuclear and cytosolic pools. Reason: The curated receptor-complex studies support nuclear and cytosolic pools. A localization annotation does not imply that this immunophilin is obligatory for androgen receptor import. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0005634 nucleus | IDA PMID:8341706 Overexpression, characterization, and purification of a reco... | ACCEPT | Summary: The curated receptor-complex studies support nuclear and cytosolic pools. Reason: The curated receptor-complex studies support nuclear and cytosolic pools. A localization annotation does not imply that this immunophilin is obligatory for androgen receptor import. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: The curated receptor-complex studies support nuclear and cytosolic pools. Reason: The curated receptor-complex studies support nuclear and cytosolic pools. A localization annotation does not imply that this immunophilin is obligatory for androgen receptor import. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0005654 nucleoplasm | ISO GO_REF:0000119 | UNDECIDED | Summary: Nuclear localization is supported, but the more specific nucleoplasmic compartment has not been independently resolved here; nuclear entry cannot establish every nuclear subcompartment. Reason: Nuclear localization is supported, but the more specific nucleoplasmic compartment has not been independently resolved here; nuclear entry cannot establish every nuclear subcompartment. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q02790 UNRESOLVED The seeded source is recorded without claiming that an unresolved source experiment or PAINT node was independently reconstructed. Nuclear localization is supported, but the more specific nucleoplasmic compartment has not been independently resolved here; nuclear entry cannot establish every nuclear subcompartment. Supporting Evidence: |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Reason: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Colocalized with MAPT/TAU in the distal part of the primary cortical neurons. |
| GO:0005739 mitochondrion | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Reason: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Colocalized with MAPT/TAU in the distal part of the primary cortical neurons. |
| GO:0005739 mitochondrion | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Reason: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Colocalized with MAPT/TAU in the distal part of the primary cortical neurons. |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: The curated receptor-complex studies support nuclear and cytosolic pools. Reason: The curated receptor-complex studies support nuclear and cytosolic pools. A localization annotation does not imply that this immunophilin is obligatory for androgen receptor import. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0005829 cytosol | IEA GO_REF:0000120 | ACCEPT | Summary: The curated receptor-complex studies support nuclear and cytosolic pools. Reason: The curated receptor-complex studies support nuclear and cytosolic pools. A localization annotation does not imply that this immunophilin is obligatory for androgen receptor import. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0005829 cytosol | ISO GO_REF:0000096 | ACCEPT | Summary: The curated receptor-complex studies support nuclear and cytosolic pools. Reason: The curated receptor-complex studies support nuclear and cytosolic pools. A localization annotation does not imply that this immunophilin is obligatory for androgen receptor import. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0005829 cytosol | ISO GO_REF:0000119 | ACCEPT | Summary: The curated receptor-complex studies support nuclear and cytosolic pools. Reason: The curated receptor-complex studies support nuclear and cytosolic pools. A localization annotation does not imply that this immunophilin is obligatory for androgen receptor import. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0005829 cytosol | ISS GO_REF:0000024 | ACCEPT | Summary: The curated receptor-complex studies support nuclear and cytosolic pools. Reason: The curated receptor-complex studies support nuclear and cytosolic pools. A localization annotation does not imply that this immunophilin is obligatory for androgen receptor import. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Reason: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Colocalized with MAPT/TAU in the distal part of the primary cortical neurons. |
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: The immunophilin participates in protein conformational maturation as a PPIase and HSP90-associated co-chaperone. Reason: The immunophilin participates in protein conformational maturation as a PPIase and HSP90-associated co-chaperone. This does not assert that every receptor effect requires the catalytic reaction. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0006457 protein folding | IEA GO_REF:0000107 | ACCEPT | Summary: The immunophilin participates in protein conformational maturation as a PPIase and HSP90-associated co-chaperone. Reason: The immunophilin participates in protein conformational maturation as a PPIase and HSP90-associated co-chaperone. This does not assert that every receptor effect requires the catalytic reaction. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0006457 protein folding | ISO GO_REF:0000119 | ACCEPT | Summary: The immunophilin participates in protein conformational maturation as a PPIase and HSP90-associated co-chaperone. Reason: The immunophilin participates in protein conformational maturation as a PPIase and HSP90-associated co-chaperone. This does not assert that every receptor effect requires the catalytic reaction. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0006457 protein folding | ISS GO_REF:0000024 | ACCEPT | Summary: The immunophilin participates in protein conformational maturation as a PPIase and HSP90-associated co-chaperone. Reason: The immunophilin participates in protein conformational maturation as a PPIase and HSP90-associated co-chaperone. This does not assert that every receptor effect requires the catalytic reaction. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0006463 steroid hormone receptor complex assembly | IDA PMID:11751894 A new first step in activation of steroid receptors: hormone... | ACCEPT | Summary: Reconstitution and hormone-dependent immunophilin exchange place FKBP52 directly in steroid-receptor heterocomplex assembly. Reason: Reconstitution and hormone-dependent immunophilin exchange place FKBP52 directly in steroid-receptor heterocomplex assembly. The exchange/import experiment concerns glucocorticoid receptor and is not universal evidence for androgen receptor import. Supporting Evidence: PMID:8341706 The rFKBP-52 can be assembled in vitro with the glucocorticoid receptor complex |
| GO:0006463 steroid hormone receptor complex assembly | IDA PMID:8341706 Overexpression, characterization, and purification of a reco... | ACCEPT | Summary: Reconstitution and hormone-dependent immunophilin exchange place FKBP52 directly in steroid-receptor heterocomplex assembly. Reason: Reconstitution and hormone-dependent immunophilin exchange place FKBP52 directly in steroid-receptor heterocomplex assembly. The exchange/import experiment concerns glucocorticoid receptor and is not universal evidence for androgen receptor import. Supporting Evidence: PMID:8341706 The rFKBP-52 can be assembled in vitro with the glucocorticoid receptor complex |
| GO:0006825 copper ion transport | IEA GO_REF:0000107 | UNDECIDED | Summary: The copper-related ortholog transfer is not resolved by the available receptor and neuronal studies. Reason: The copper-related ortholog transfer is not resolved by the available receptor and neuronal studies. Neither the immunophilin name nor a generic metal-binding prediction establishes copper transport or copper-dependent binding. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0006825 copper ion transport | ISO GO_REF:0000096 | UNDECIDED | Summary: The copper-related ortholog transfer is not resolved by the available receptor and neuronal studies. Reason: The copper-related ortholog transfer is not resolved by the available receptor and neuronal studies. Neither the immunophilin name nor a generic metal-binding prediction establishes copper transport or copper-dependent binding. Propagation Review Root cause: UNRESOLVED Sources checked: RGD:628729 UNRESOLVED The seeded source is recorded without claiming that an unresolved source experiment or PAINT node was independently reconstructed. The copper-related ortholog transfer is not resolved by the available receptor and neuronal studies. Neither the immunophilin name nor a generic metal-binding prediction establishes copper transport or copper-dependent binding. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0007566 embryo implantation | IMP PMID:17142810 Essential role for Co-chaperone Fkbp52 but not Fkbp51 in and... | UNDECIDED | Summary: The supplied paper chiefly resolves male AR physiology. Reason: The supplied paper chiefly resolves male AR physiology. Its accessible abstract does not adjudicate the embryo-implantation experiment; absence from that abstract is not evidence against an experimentally curated female reproductive role. Supporting Evidence: |
| GO:0010977 negative regulation of neuron projection development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: FKBP52 binds Tau and antagonizes Tau-dependent microtubule assembly; neurite-growth effects are a separate, context-dependent function from steroid-receptor co-chaperoning. Reason: FKBP52 binds Tau and antagonizes Tau-dependent microtubule assembly; neurite-growth effects are a separate, context-dependent function from steroid-receptor co-chaperoning. The conserved ortholog inference is supported by direct biochemical and neuronal evidence, without labeling those experiments as mouse knockouts. Supporting Evidence: PMID:20133804 FKBP52, which is abundant in brain, binds directly and specifically to Tau |
| GO:0030521 androgen receptor signaling pathway | IMP PMID:17142810 Essential role for Co-chaperone Fkbp52 but not Fkbp51 in and... | ACCEPT | Summary: Mouse Fkbp4 loss impairs AR-dependent transcription and selective reproductive tissues, while AR ligand binding and nuclear translocation remain intact. Reason: Mouse Fkbp4 loss impairs AR-dependent transcription and selective reproductive tissues, while AR ligand binding and nuclear translocation remain intact. FKBP52 executes a co-chaperone contribution to signaling rather than the receptor DNA-binding step. Supporting Evidence: PMID:17142810 Fkbp52 is critical to AR transcriptional activity. |
| GO:0030850 prostate gland development | IMP PMID:17142810 Essential role for Co-chaperone Fkbp52 but not Fkbp51 in and... | KEEP AS NON CORE | Summary: Native Fkbp4-null mice show tissue-selective male reproductive abnormalities, including prostate dysgenesis and penile hypospadias. Reason: Native Fkbp4-null mice show tissue-selective male reproductive abnormalities, including prostate dysgenesis and penile hypospadias. These developmental consequences are peripheral to the co-chaperone molecular function; testicular failure is not implied. |
| GO:0031072 heat shock protein binding | IDA PMID:8341706 Overexpression, characterization, and purification of a reco... | ACCEPT | Summary: HSP90 association recruits the immunophilin to steroid-receptor heterocomplexes and is central to its co-chaperone role. Reason: HSP90 association recruits the immunophilin to steroid-receptor heterocomplexes and is central to its co-chaperone role. Supporting Evidence: |
| GO:0031072 heat shock protein binding | IEA GO_REF:0000107 | ACCEPT | Summary: HSP90 association recruits the immunophilin to steroid-receptor heterocomplexes and is central to its co-chaperone role. Reason: HSP90 association recruits the immunophilin to steroid-receptor heterocomplexes and is central to its co-chaperone role. Supporting Evidence: |
| GO:0031072 heat shock protein binding | ISO GO_REF:0000119 | ACCEPT | Summary: HSP90 association recruits the immunophilin to steroid-receptor heterocomplexes and is central to its co-chaperone role. Reason: HSP90 association recruits the immunophilin to steroid-receptor heterocomplexes and is central to its co-chaperone role. Supporting Evidence: |
| GO:0031111 negative regulation of microtubule polymerization or depolymerization | ISS GO_REF:0000024 | MODIFY | Summary: The supported microtubule effect is inhibition of polymerization. Reason: FKBP52 antagonizes Tau-dependent microtubule assembly. Refine the broader polymerization-or-depolymerization term to the supported negative regulation of polymerization. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB:P27124 SUPPORTS TRANSFER The source assertion was assessed against target-specific mechanistic evidence. FKBP52 antagonizes Tau-dependent microtubule assembly. Refine the broader polymerization-or-depolymerization term to the supported negative regulation of polymerization. Proposed replacements: negative regulation of microtubule polymerization Supporting Evidence: PMID:20133804 FKBP52, which is abundant in brain, binds directly and specifically to Tau |
| GO:0031115 negative regulation of microtubule polymerization | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: FKBP52 binds Tau and antagonizes Tau-dependent microtubule assembly; neurite-growth effects are a separate, context-dependent function from steroid-receptor co-chaperoning. Reason: FKBP52 binds Tau and antagonizes Tau-dependent microtubule assembly; neurite-growth effects are a separate, context-dependent function from steroid-receptor co-chaperoning. The conserved ortholog inference is supported by direct biochemical and neuronal evidence, without labeling those experiments as mouse knockouts. Supporting Evidence: PMID:20133804 FKBP52, which is abundant in brain, binds directly and specifically to Tau |
| GO:0031115 negative regulation of microtubule polymerization | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: FKBP52 binds Tau and antagonizes Tau-dependent microtubule assembly; neurite-growth effects are a separate, context-dependent function from steroid-receptor co-chaperoning. Reason: FKBP52 binds Tau and antagonizes Tau-dependent microtubule assembly; neurite-growth effects are a separate, context-dependent function from steroid-receptor co-chaperoning. The conserved ortholog inference is supported by direct biochemical and neuronal evidence, without labeling those experiments as mouse knockouts. Supporting Evidence: PMID:20133804 FKBP52, which is abundant in brain, binds directly and specifically to Tau |
| GO:0031503 protein-containing complex localization | IDA PMID:11751894 A new first step in activation of steroid receptors: hormone... | ACCEPT | Summary: FKBP52 participates in localization of the glucocorticoid receptor-HSP90-dynein complex before its nuclear dissociation. Reason: FKBP52 participates in localization of the glucocorticoid receptor-HSP90-dynein complex before its nuclear dissociation. This is directly supported for that complex; mouse AR ligand binding and import persist after Fkbp4 loss. |
| GO:0032767 copper-dependent protein binding | IEA GO_REF:0000107 | UNDECIDED | Summary: The copper-related ortholog transfer is not resolved by the available receptor and neuronal studies. Reason: The copper-related ortholog transfer is not resolved by the available receptor and neuronal studies. Neither the immunophilin name nor a generic metal-binding prediction establishes copper transport or copper-dependent binding. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0032767 copper-dependent protein binding | ISO GO_REF:0000096 | UNDECIDED | Summary: The copper-related ortholog transfer is not resolved by the available receptor and neuronal studies. Reason: The copper-related ortholog transfer is not resolved by the available receptor and neuronal studies. Neither the immunophilin name nor a generic metal-binding prediction establishes copper transport or copper-dependent binding. Propagation Review Root cause: UNRESOLVED Sources checked: RGD:628729 UNRESOLVED The seeded source is recorded without claiming that an unresolved source experiment or PAINT node was independently reconstructed. The copper-related ortholog transfer is not resolved by the available receptor and neuronal studies. Neither the immunophilin name nor a generic metal-binding prediction establishes copper transport or copper-dependent binding. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Immunophilin protein with PPIase and co-chaperone activities. |
| GO:0032991 protein-containing complex | IEA GO_REF:0000107 | UNDECIDED | Summary: Membership in receptor heterocomplexes is established, but this generic complex annotation may represent a distinct transferred complex. Reason: Membership in receptor heterocomplexes is established, but this generic complex annotation may represent a distinct transferred complex. Its intended specific assembly cannot be recovered from the available evidence. Supporting Evidence: |
| GO:0032991 protein-containing complex | ISO GO_REF:0000096 | UNDECIDED | Summary: Membership in receptor heterocomplexes is established, but this generic complex annotation may represent a distinct transferred complex. Reason: Membership in receptor heterocomplexes is established, but this generic complex annotation may represent a distinct transferred complex. Its intended specific assembly cannot be recovered from the available evidence. Propagation Review Root cause: UNRESOLVED Sources checked: RGD:628729 UNRESOLVED The seeded source is recorded without claiming that an unresolved source experiment or PAINT node was independently reconstructed. Membership in receptor heterocomplexes is established, but this generic complex annotation may represent a distinct transferred complex. Its intended specific assembly cannot be recovered from the available evidence. Supporting Evidence: |
| GO:0035259 obsolete nuclear glucocorticoid receptor binding | IDA PMID:7693550 Cloning and expression of a mouse cDNA encoding p59, an immu... | MODIFY | Summary: Direct glucocorticoid receptor association is supported. Reason: Direct glucocorticoid receptor association is supported. QuickGO confirms that the seeded specialized term is obsolete; preserve its original identifier while proposing the current signaling receptor binding term for the established interaction. Proposed replacements: signaling receptor binding |
| GO:0035259 obsolete nuclear glucocorticoid receptor binding | IDA PMID:8341706 Overexpression, characterization, and purification of a reco... | MODIFY | Summary: Direct glucocorticoid receptor association is supported. Reason: Direct glucocorticoid receptor association is supported. QuickGO confirms that the seeded specialized term is obsolete; preserve its original identifier while proposing the current signaling receptor binding term for the established interaction. Proposed replacements: signaling receptor binding |
| GO:0043025 neuronal cell body | IEA GO_REF:0000107 | UNDECIDED | Summary: The precise neuronal cell-body or perinuclear localization is not resolved by the available target-specific evidence; broad cytoplasmic localization is insufficient. Reason: The precise neuronal cell-body or perinuclear localization is not resolved by the available target-specific evidence; broad cytoplasmic localization is insufficient. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Colocalized with MAPT/TAU in the distal part of the primary cortical neurons. |
| GO:0043025 neuronal cell body | ISO GO_REF:0000096 | UNDECIDED | Summary: The precise neuronal cell-body or perinuclear localization is not resolved by the available target-specific evidence; broad cytoplasmic localization is insufficient. Reason: The precise neuronal cell-body or perinuclear localization is not resolved by the available target-specific evidence; broad cytoplasmic localization is insufficient. Propagation Review Root cause: UNRESOLVED Sources checked: RGD:628729 UNRESOLVED The seeded source is recorded without claiming that an unresolved source experiment or PAINT node was independently reconstructed. The precise neuronal cell-body or perinuclear localization is not resolved by the available target-specific evidence; broad cytoplasmic localization is insufficient. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Colocalized with MAPT/TAU in the distal part of the primary cortical neurons. |
| GO:0044295 axonal growth cone | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Reason: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Colocalized with MAPT/TAU in the distal part of the primary cortical neurons. |
| GO:0044295 axonal growth cone | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Reason: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Colocalized with MAPT/TAU in the distal part of the primary cortical neurons. |
| GO:0044295 axonal growth cone | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Reason: Curated localization and neuronal studies support additional mitochondrial or cytoskeletal pools and distal-neurite association, peripheral to receptor co-chaperoning. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Colocalized with MAPT/TAU in the distal part of the primary cortical neurons. |
| GO:0046661 male sex differentiation | IMP PMID:15831525 Physiological role for the cochaperone FKBP52 in androgen re... | KEEP AS NON CORE | Summary: Native Fkbp4-null mice show tissue-selective male reproductive abnormalities, including prostate dysgenesis and penile hypospadias. Reason: Native Fkbp4-null mice show tissue-selective male reproductive abnormalities, including prostate dysgenesis and penile hypospadias. These developmental consequences are peripheral to the co-chaperone molecular function; testicular failure is not implied. |
| GO:0048156 tau protein binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: FKBP52 binds Tau and antagonizes Tau-dependent microtubule assembly; neurite-growth effects are a separate, context-dependent function from steroid-receptor co-chaperoning. Reason: FKBP52 binds Tau and antagonizes Tau-dependent microtubule assembly; neurite-growth effects are a separate, context-dependent function from steroid-receptor co-chaperoning. The conserved ortholog inference is supported by direct biochemical and neuronal evidence, without labeling those experiments as mouse knockouts. Supporting Evidence: PMID:20133804 FKBP52, which is abundant in brain, binds directly and specifically to Tau |
| GO:0048156 tau protein binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: FKBP52 binds Tau and antagonizes Tau-dependent microtubule assembly; neurite-growth effects are a separate, context-dependent function from steroid-receptor co-chaperoning. Reason: FKBP52 binds Tau and antagonizes Tau-dependent microtubule assembly; neurite-growth effects are a separate, context-dependent function from steroid-receptor co-chaperoning. The conserved ortholog inference is supported by direct biochemical and neuronal evidence, without labeling those experiments as mouse knockouts. Supporting Evidence: PMID:20133804 FKBP52, which is abundant in brain, binds directly and specifically to Tau |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000107 | UNDECIDED | Summary: The precise neuronal cell-body or perinuclear localization is not resolved by the available target-specific evidence; broad cytoplasmic localization is insufficient. Reason: The precise neuronal cell-body or perinuclear localization is not resolved by the available target-specific evidence; broad cytoplasmic localization is insufficient. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Colocalized with MAPT/TAU in the distal part of the primary cortical neurons. |
| GO:0048471 perinuclear region of cytoplasm | ISO GO_REF:0000096 | UNDECIDED | Summary: The precise neuronal cell-body or perinuclear localization is not resolved by the available target-specific evidence; broad cytoplasmic localization is insufficient. Reason: The precise neuronal cell-body or perinuclear localization is not resolved by the available target-specific evidence; broad cytoplasmic localization is insufficient. Propagation Review Root cause: UNRESOLVED Sources checked: RGD:628729 UNRESOLVED The seeded source is recorded without claiming that an unresolved source experiment or PAINT node was independently reconstructed. The precise neuronal cell-body or perinuclear localization is not resolved by the available target-specific evidence; broad cytoplasmic localization is insufficient. Supporting Evidence: file:mouse/Fkbp4/Fkbp4-uniprot.txt Colocalized with MAPT/TAU in the distal part of the primary cortical neurons. |
| GO:0048608 reproductive structure development | IMP PMID:17142810 Essential role for Co-chaperone Fkbp52 but not Fkbp51 in and... | KEEP AS NON CORE | Summary: Native Fkbp4-null mice show tissue-selective male reproductive abnormalities, including prostate dysgenesis and penile hypospadias. Reason: Native Fkbp4-null mice show tissue-selective male reproductive abnormalities, including prostate dysgenesis and penile hypospadias. These developmental consequences are peripheral to the co-chaperone molecular function; testicular failure is not implied. |
| GO:0051219 phosphoprotein binding | IDA PMID:8341706 Overexpression, characterization, and purification of a reco... | KEEP AS NON CORE | Summary: Purified recombinant mouse FKBP52 co-purifies with a 59-kDa phosphoprotein/kinase. Reason: Purified recombinant mouse FKBP52 co-purifies with a 59-kDa phosphoprotein/kinase. Retain the reported phosphoprotein association as peripheral; the co-purifying kinase does not establish that FKBP52 itself phosphorylates substrates. Supporting Evidence: PMID:8341706 a phosphoprotein or kinase that is associated with the rFKBP-52 |
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