BIN1 encodes amphiphysin II, a BAR/N-BAR and SH3-domain membrane-remodeling adaptor with extensive alternative splicing in brain and skeletal muscle. BIN1 binds phospholipid membranes, senses and generates membrane curvature, promotes lipid tubulation, and organizes membrane domains used in endocytosis, synaptic-vesicle cycling, endosomal sorting, and skeletal-muscle T-tubule formation. Through SH3-domain interactions with endocytic proteins such as dynamin and clathrin/AP2-associated machinery, BIN1 links curved membranes to vesicle trafficking and cytoskeletal organization. Additional context-specific functions include nuclear/MYC-related tumor-suppressor activities, tau and clusterin interactions, and regulation of BACE1 trafficking and amyloid-beta production.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0008021 synaptic vesicle | IBA GO_REF:0000033 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0005543 phospholipid binding | IBA GO_REF:0000033 | ACCEPT | Summary: BIN1 BAR/N-BAR domains bind phospholipid membranes and generate or sense membrane curvature. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0048156 tau protein binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: BIN1-tau interaction is experimentally supported and Alzheimer-relevant, but it is a context-specific disease/pathology interaction rather than the primary BAR-domain membrane-remodeling role. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: This nuclear, transcriptional, cell-cycle, differentiation, or apoptotic annotation reflects tumor-suppressor/isoform-specific or downstream contexts, not the main BIN1 membrane-remodeling function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005768 endosome | IEA GO_REF:0000044 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0006897 endocytosis | IEA GO_REF:0000117 | ACCEPT | Summary: BIN1 functions as an endocytic adaptor through clathrin/AP2/dynamin-related interactions and membrane remodeling. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0016020 membrane | IEA GO_REF:0000117 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0030100 regulation of endocytosis | IEA GO_REF:0000002 | ACCEPT | Summary: BIN1 functions as an endocytic adaptor through clathrin/AP2/dynamin-related interactions and membrane remodeling. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0030315 T-tubule | IEA GO_REF:0000120 | ACCEPT | Summary: BIN1 is required for muscle membrane organization, especially T-tubule formation and associated sarcomeric membrane domains. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0030424 axon | IEA GO_REF:0000117 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0051649 establishment of localization in cell | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: This process is too broad for BIN1 compared with specific endocytosis, vesicle sorting, and membrane-remodeling terms. Reason: Use more informative trafficking/endocytosis and membrane-remodeling terms instead of broad establishment of localization in cell. |
| GO:0005515 protein binding | IPI PMID:10903846 Bin2, a functionally nonredundant member of the BAR adaptor ... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:12604805 Identification and characterization of amphiphysin II as a n... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:12668730 Sorting nexin 4 and amphiphysin 2, a new partnership between... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:16275660 Identification of VCP/p97, carboxyl terminus of Hsp70-intera... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:16530520 The SH3 binding motif of HCV [corrected] NS5A protein intera... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:18647389 The central proline rich region of POB1/REPS2 plays a regula... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:18985028 Hepatitis C virus infection protein network. | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:23917616 The myotubularin-amphiphysin 2 complex in membrane tubulatio... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:24169621 Elucidating novel hepatitis C virus-host interactions using ... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:31413325 HENA, heterogeneous network-based data set for Alzheimer's d... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:32552912 Upregulation of RIN3 induces endosomal dysfunction in Alzhei... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0042802 identical protein binding | IPI PMID:23917616 The myotubularin-amphiphysin 2 complex in membrane tubulatio... | KEEP AS NON CORE | Summary: This annotation is plausible or supported, but it is more context-specific or less informative than the core BIN1 membrane-remodeling/endocytic functions. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0042802 identical protein binding | IPI PMID:31413325 HENA, heterogeneous network-based data set for Alzheimer's d... | KEEP AS NON CORE | Summary: This annotation is plausible or supported, but it is more context-specific or less informative than the core BIN1 membrane-remodeling/endocytic functions. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0008021 synaptic vesicle | IEA GO_REF:0000107 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0030018 Z disc | IEA GO_REF:0000107 | ACCEPT | Summary: BIN1 is required for muscle membrane organization, especially T-tubule formation and associated sarcomeric membrane domains. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0031674 I band | IEA GO_REF:0000107 | ACCEPT | Summary: BIN1 is required for muscle membrane organization, especially T-tubule formation and associated sarcomeric membrane domains. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0033268 node of Ranvier | IEA GO_REF:0000107 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0043194 axon initial segment | IEA GO_REF:0000107 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0043196 varicosity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: This annotation is plausible or supported, but it is more context-specific or less informative than the core BIN1 membrane-remodeling/endocytic functions. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0043679 axon terminus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: This annotation is plausible or supported, but it is more context-specific or less informative than the core BIN1 membrane-remodeling/endocytic functions. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0044300 cerebellar mossy fiber | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: This annotation is plausible or supported, but it is more context-specific or less informative than the core BIN1 membrane-remodeling/endocytic functions. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0044877 protein-containing complex binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: This annotation is plausible or supported, but it is more context-specific or less informative than the core BIN1 membrane-remodeling/endocytic functions. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0045807 positive regulation of endocytosis | IEA GO_REF:0000107 | ACCEPT | Summary: BIN1 functions as an endocytic adaptor through clathrin/AP2/dynamin-related interactions and membrane remodeling. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0048488 synaptic vesicle endocytosis | IEA GO_REF:0000107 | ACCEPT | Summary: BIN1 functions as an endocytic adaptor through clathrin/AP2/dynamin-related interactions and membrane remodeling. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0051020 GTPase binding | IEA GO_REF:0000107 | ACCEPT | Summary: BIN1 functions as an endocytic adaptor through clathrin/AP2/dynamin-related interactions and membrane remodeling. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0098850 extrinsic component of synaptic vesicle membrane | IEA GO_REF:0000107 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0098978 glutamatergic synapse | IEA GO_REF:0000107 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0000122 negative regulation of transcription by RNA polymerase II | IDA PMID:10412034 Induction of apoptosis and differentiation in neuroblastoma ... | KEEP AS NON CORE | Summary: This nuclear, transcriptional, cell-cycle, differentiation, or apoptotic annotation reflects tumor-suppressor/isoform-specific or downstream contexts, not the main BIN1 membrane-remodeling function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0005634 nucleus | IDA PMID:8782822 BIN1 is a novel MYC-interacting protein with features of a t... | KEEP AS NON CORE | Summary: This nuclear, transcriptional, cell-cycle, differentiation, or apoptotic annotation reflects tumor-suppressor/isoform-specific or downstream contexts, not the main BIN1 membrane-remodeling function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0010564 regulation of cell cycle process | IDA PMID:8782822 BIN1 is a novel MYC-interacting protein with features of a t... | KEEP AS NON CORE | Summary: This nuclear, transcriptional, cell-cycle, differentiation, or apoptotic annotation reflects tumor-suppressor/isoform-specific or downstream contexts, not the main BIN1 membrane-remodeling function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0090571 RNA polymerase II transcription repressor complex | IPI PMID:15992821 A structure-based model of the c-Myc/Bin1 protein interactio... | KEEP AS NON CORE | Summary: This nuclear, transcriptional, cell-cycle, differentiation, or apoptotic annotation reflects tumor-suppressor/isoform-specific or downstream contexts, not the main BIN1 membrane-remodeling function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0005737 cytoplasm | EXP PMID:9182667 Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rv... | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005768 endosome | ISS GO_REF:0000024 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0008289 lipid binding | EXP PMID:18658220 Structure and dynamics of helix-0 of the N-BAR domain in lip... | ACCEPT | Summary: BIN1 BAR/N-BAR domains bind phospholipid membranes and generate or sense membrane curvature. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0060988 lipid tube assembly | IDA PMID:18658220 Structure and dynamics of helix-0 of the N-BAR domain in lip... | ACCEPT | Summary: BIN1 has intrinsic membrane-tubulating activity and supports lipid tube or membrane tubule formation. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:1901380 negative regulation of potassium ion transmembrane transport | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: This annotation is plausible or supported, but it is more context-specific or less informative than the core BIN1 membrane-remodeling/endocytic functions. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:1903946 negative regulation of ventricular cardiac muscle cell action potential | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: This annotation is plausible or supported, but it is more context-specific or less informative than the core BIN1 membrane-remodeling/endocytic functions. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0030838 positive regulation of actin filament polymerization | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: This annotation is plausible or supported, but it is more context-specific or less informative than the core BIN1 membrane-remodeling/endocytic functions. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0086091 regulation of heart rate by cardiac conduction | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: This annotation is plausible or supported, but it is more context-specific or less informative than the core BIN1 membrane-remodeling/endocytic functions. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:1904878 negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: This annotation is plausible or supported, but it is more context-specific or less informative than the core BIN1 membrane-remodeling/endocytic functions. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0030424 axon | ISS PMID:32552912 Upregulation of RIN3 induces endosomal dysfunction in Alzhei... | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0030425 dendrite | ISS PMID:32552912 Upregulation of RIN3 induces endosomal dysfunction in Alzhei... | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0031982 vesicle | ISS PMID:32552912 Upregulation of RIN3 induces endosomal dysfunction in Alzhei... | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0019828 aspartic-type endopeptidase inhibitor activity | IMP PMID:27179792 BIN1 regulates BACE1 intracellular trafficking and amyloid-Ξ²... | MODIFY | Summary: BIN1 regulates BACE1 abundance and amyloid-beta production by endosomal trafficking and lysosomal degradation, not by acting as a direct aspartic protease inhibitor. Reason: Replace direct aspartic-type endopeptidase inhibitor activity with protease binding plus BACE1 trafficking/amyloid-output process terms. Proposed replacements: protease binding endosome to lysosome transport negative regulation of amyloid-beta formation |
| GO:1902430 negative regulation of amyloid-beta formation | IMP PMID:27179792 BIN1 regulates BACE1 intracellular trafficking and amyloid-Ξ²... | KEEP AS NON CORE | Summary: BIN1 regulation of BACE1 trafficking and amyloid-beta production is supported, but is a cargo-specific Alzheimer-relevant context rather than the core BIN1 function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0008333 endosome to lysosome transport | IMP PMID:27179792 BIN1 regulates BACE1 intracellular trafficking and amyloid-Ξ²... | KEEP AS NON CORE | Summary: BIN1 regulation of BACE1 trafficking and amyloid-beta production is supported, but is a cargo-specific Alzheimer-relevant context rather than the core BIN1 function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0048156 tau protein binding | NAS PMID:28386764 Roles of tau protein in health and disease. | KEEP AS NON CORE | Summary: BIN1-tau interaction is experimentally supported and Alzheimer-relevant, but it is a context-specific disease/pathology interaction rather than the primary BAR-domain membrane-remodeling role. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0005515 protein binding | IPI PMID:17676042 Mutations in amphiphysin 2 (BIN1) disrupt interaction with d... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0033292 T-tubule organization | IDA PMID:24755653 Mutations in BIN1 associated with centronuclear myopathy dis... | ACCEPT | Summary: BIN1 is required for muscle membrane organization, especially T-tubule formation and associated sarcomeric membrane domains. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0030315 T-tubule | ISS GO_REF:0000024 | ACCEPT | Summary: BIN1 is required for muscle membrane organization, especially T-tubule formation and associated sarcomeric membrane domains. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0033292 T-tubule organization | ISS GO_REF:0000024 | ACCEPT | Summary: BIN1 is required for muscle membrane organization, especially T-tubule formation and associated sarcomeric membrane domains. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0002020 protease binding | IPI PMID:27179792 BIN1 regulates BACE1 intracellular trafficking and amyloid-Ξ²... | KEEP AS NON CORE | Summary: BIN1 regulation of BACE1 trafficking and amyloid-beta production is supported, but is a cargo-specific Alzheimer-relevant context rather than the core BIN1 function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0005634 nucleus | IDA PMID:25051234 Intracellular clusterin interacts with brain isoforms of the... | KEEP AS NON CORE | Summary: This nuclear, transcriptional, cell-cycle, differentiation, or apoptotic annotation reflects tumor-suppressor/isoform-specific or downstream contexts, not the main BIN1 membrane-remodeling function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0005737 cytoplasm | IDA PMID:25051234 Intracellular clusterin interacts with brain isoforms of the... | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005856 cytoskeleton | IDA PMID:25051234 Intracellular clusterin interacts with brain isoforms of the... | ACCEPT | Summary: BIN1 couples membrane remodeling to the actin/cytoskeletal system, including direct actin filament binding/remodeling evidence. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0006897 endocytosis | TAS PMID:23399914 Increased expression of BIN1 mediates Alzheimer genetic risk... | ACCEPT | Summary: BIN1 functions as an endocytic adaptor through clathrin/AP2/dynamin-related interactions and membrane remodeling. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0006897 endocytosis | TAS PMID:25051234 Intracellular clusterin interacts with brain isoforms of the... | ACCEPT | Summary: BIN1 functions as an endocytic adaptor through clathrin/AP2/dynamin-related interactions and membrane remodeling. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0007010 cytoskeleton organization | TAS PMID:23399914 Increased expression of BIN1 mediates Alzheimer genetic risk... | ACCEPT | Summary: BIN1 couples membrane remodeling to the actin/cytoskeletal system, including direct actin filament binding/remodeling evidence. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0016020 membrane | IDA PMID:25051234 Intracellular clusterin interacts with brain isoforms of the... | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0016020 membrane | TAS PMID:28755476 Regulation of the interaction between the neuronal BIN1 isof... | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0030276 clathrin binding | TAS PMID:25051234 Intracellular clusterin interacts with brain isoforms of the... | ACCEPT | Summary: BIN1 functions as an endocytic adaptor through clathrin/AP2/dynamin-related interactions and membrane remodeling. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0048156 tau protein binding | IPI PMID:25051234 Intracellular clusterin interacts with brain isoforms of the... | KEEP AS NON CORE | Summary: BIN1-tau interaction is experimentally supported and Alzheimer-relevant, but it is a context-specific disease/pathology interaction rather than the primary BAR-domain membrane-remodeling role. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0051087 protein-folding chaperone binding | IPI PMID:25051234 Intracellular clusterin interacts with brain isoforms of the... | KEEP AS NON CORE | Summary: This annotation is plausible or supported, but it is more context-specific or less informative than the core BIN1 membrane-remodeling/endocytic functions. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8867754 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868230 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868236 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868648 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868651 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868658 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868659 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868660 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8868661 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8869438 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8871193 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8871194 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0005515 protein binding | IPI PMID:26506308 Amphiphysin 2 Orchestrates Nucleus Positioning and Shape by ... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0006997 nucleus organization | IMP PMID:26506308 Amphiphysin 2 Orchestrates Nucleus Positioning and Shape by ... | KEEP AS NON CORE | Summary: This nuclear, transcriptional, cell-cycle, differentiation, or apoptotic annotation reflects tumor-suppressor/isoform-specific or downstream contexts, not the main BIN1 membrane-remodeling function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0051015 actin filament binding | IDA PMID:26506308 Amphiphysin 2 Orchestrates Nucleus Positioning and Shape by ... | ACCEPT | Summary: BIN1 couples membrane remodeling to the actin/cytoskeletal system, including direct actin filament binding/remodeling evidence. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0016020 membrane | IDA PMID:16530520 The SH3 binding motif of HCV [corrected] NS5A protein intera... | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0043065 positive regulation of apoptotic process | IDA PMID:16530520 The SH3 binding motif of HCV [corrected] NS5A protein intera... | KEEP AS NON CORE | Summary: This nuclear, transcriptional, cell-cycle, differentiation, or apoptotic annotation reflects tumor-suppressor/isoform-specific or downstream contexts, not the main BIN1 membrane-remodeling function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0070063 RNA polymerase binding | IPI PMID:16530520 The SH3 binding motif of HCV [corrected] NS5A protein intera... | KEEP AS NON CORE | Summary: This nuclear, transcriptional, cell-cycle, differentiation, or apoptotic annotation reflects tumor-suppressor/isoform-specific or downstream contexts, not the main BIN1 membrane-remodeling function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0030018 Z disc | ISS GO_REF:0000024 | ACCEPT | Summary: BIN1 is required for muscle membrane organization, especially T-tubule formation and associated sarcomeric membrane domains. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0031674 I band | ISS GO_REF:0000024 | ACCEPT | Summary: BIN1 is required for muscle membrane organization, especially T-tubule formation and associated sarcomeric membrane domains. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0033268 node of Ranvier | ISS GO_REF:0000024 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0043194 axon initial segment | ISS GO_REF:0000024 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0043065 positive regulation of apoptotic process | IMP PMID:10412034 Induction of apoptosis and differentiation in neuroblastoma ... | KEEP AS NON CORE | Summary: This nuclear, transcriptional, cell-cycle, differentiation, or apoptotic annotation reflects tumor-suppressor/isoform-specific or downstream contexts, not the main BIN1 membrane-remodeling function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0048711 positive regulation of astrocyte differentiation | IMP PMID:10412034 Induction of apoptosis and differentiation in neuroblastoma ... | KEEP AS NON CORE | Summary: This nuclear, transcriptional, cell-cycle, differentiation, or apoptotic annotation reflects tumor-suppressor/isoform-specific or downstream contexts, not the main BIN1 membrane-remodeling function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0005515 protein binding | IPI PMID:19004523 The membrane-tubulating potential of amphiphysin 2/BIN1 is d... | MARK AS OVER ANNOTATED | Summary: The interaction may be real, but generic protein binding is not an informative molecular-function annotation for BIN1. Reason: Prefer specific BIN1 functions such as phospholipid binding, clathrin binding, GTPase/dynamin binding, actin filament binding, and membrane tubulation. |
| GO:0060987 lipid tube | IMP PMID:19004523 The membrane-tubulating potential of amphiphysin 2/BIN1 is d... | ACCEPT | Summary: BIN1 has intrinsic membrane-tubulating activity and supports lipid tube or membrane tubule formation. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0060988 lipid tube assembly | IMP PMID:19004523 The membrane-tubulating potential of amphiphysin 2/BIN1 is d... | ACCEPT | Summary: BIN1 has intrinsic membrane-tubulating activity and supports lipid tube or membrane tubule formation. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0030424 axon | IDA PMID:23399914 Increased expression of BIN1 mediates Alzheimer genetic risk... | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
| GO:0045664 regulation of neuron differentiation | IMP PMID:10412034 Induction of apoptosis and differentiation in neuroblastoma ... | KEEP AS NON CORE | Summary: This nuclear, transcriptional, cell-cycle, differentiation, or apoptotic annotation reflects tumor-suppressor/isoform-specific or downstream contexts, not the main BIN1 membrane-remodeling function. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0048156 tau protein binding | IPI PMID:23399914 Increased expression of BIN1 mediates Alzheimer genetic risk... | KEEP AS NON CORE | Summary: BIN1-tau interaction is experimentally supported and Alzheimer-relevant, but it is a context-specific disease/pathology interaction rather than the primary BAR-domain membrane-remodeling role. Reason: Retain as non-core because the annotation is supported or plausible but represents a context-specific cargo, disease, nuclear/tumor-suppressor, or downstream phenotype rather than BIN1 primary membrane-remodeling function. |
| GO:0005737 cytoplasm | IDA GO_REF:0000054 | ACCEPT | Summary: This location or process is consistent with BIN1 membrane-remodeling and endocytic adaptor function in neuronal and muscle contexts. Reason: This location is consistent with BIN1 isoform-specific function at cytosolic membrane interfaces, endosomes/synaptic vesicles, neuronal axon domains, and skeletal-muscle T-tubules. |
| GO:0015629 actin cytoskeleton | TAS PMID:9182667 Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rv... | ACCEPT | Summary: BIN1 couples membrane remodeling to the actin/cytoskeletal system, including direct actin filament binding/remodeling evidence. Reason: The term aligns with BIN1/amphiphysin II core biology as a BAR-domain and SH3-domain membrane-remodeling adaptor involved in membrane curvature, lipid tubulation, endocytosis, synaptic-vesicle domains, and muscle T-tubule organization. |
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Download this section (compressed HTML)Q: Which BIN1 isoforms should be treated as functionally distinct for GO curation of neuronal endocytosis, skeletal-muscle T-tubule biogenesis, and nuclear/MYC-associated activities?
Suggested experts: BIN1 isoform experts, GO membrane trafficking curators
Q: Should BIN1 regulation of BACE1 abundance be curated as cargo-specific endosomal sorting rather than as direct aspartic protease inhibitor activity?
Suggested experts: APP/BACE1 trafficking experts, GO molecular-function curators
Experiment: Rescue BIN1-null human neurons and myotubes with endogenous-level brain and muscle isoforms, then quantify clathrin/AP2/dynamin recruitment, membrane tubulation, endocytosis, and T-tubule organization.
Hypothesis: BIN1 isoform-specific inserts tune a shared BAR/SH3 membrane-remodeling module toward neuronal endocytosis or skeletal-muscle T-tubule formation.
Type: endogenous isoform-rescue membrane-remodeling assay
Experiment: Separate BIN1-BACE1 binding from endosomal sorting by comparing BAR-domain, SH3-domain, and BACE1-binding mutants for BACE1 lysosomal delivery and amyloid-beta production.
Hypothesis: BIN1 reduces amyloid-beta output primarily by BACE1 trafficking and lysosomal degradation rather than direct protease inhibition.
Type: cargo-specific trafficking separation-of-function assay
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