BLOC1S6, also called pallidin, is a small coiled-coil protein in the eight-subunit BLOC-1 complex. It forms a stable assembly with BLOS1 and Cappuccino and links this machinery to membrane-trafficking proteins, including syntaxins. Pallidin occurs in cytosolic and peripheral membrane-associated pools. BLOC-1 supports sorting of endosomal cargo toward melanosomes and other lysosome-related organelles, including platelet dense granules. Human pallidin restores pigmentation and cargo sorting in pallid mouse melanocytes. Pallidin-containing complexes also support selected neuronal cargo-trafficking and neurite-development functions. Biallelic BLOC1S6 defects are associated with Hermansky-Pudlak syndrome type 9; the cellular and clinical manifestations vary with the experimental and patient context.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001525 angiogenesis | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific angiogenesis assertion requires its unresolved source context. Reason: The exact mouse vascular assay was not recovered. Endosomal trafficking alone does not resolve endothelial sprouting or vessel formation. |
| GO:0001725 stress fiber | IBA GO_REF:0000033 | UNDECIDED | Summary: The specific stress fiber assertion requires its unresolved source context. Reason: The PAINT placement and its mouse stress-fiber localization experiment remain unresolved. Human overexpression in PMID:12019270 preferentially marks perinuclear actin, with less obvious long-stress-fiber labeling; this context does not contradict an uninspected mouse assay or prove loss of the ancestral function. Supporting Evidence: |
| GO:0001725 stress fiber | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific stress fiber assertion requires its unresolved source context. Reason: The exact mouse stress-fiber localization experiment remains unresolved. Selected human tagged-protein localization at perinuclear actin cannot substitute for that assay or establish a species-specific absence. Supporting Evidence: |
| GO:0001726 ruffle | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific ruffle assertion requires its unresolved source context. Reason: Tagged human perinuclear actin association does not establish the source mouse ruffle localization; the specific donor assay remains unverified. Supporting Evidence: |
| GO:0001822 kidney development | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific kidney development assertion requires its unresolved source context. Reason: Pallid mice have abnormal renal lysosomal-enzyme levels, but that phenotype alone does not establish a kidney-development mechanism. The actual developmental donor experiment remains unverified. |
| GO:0001944 vasculature development | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific vasculature development assertion requires its unresolved source context. Reason: The exact donor vessel-development experiment was not recovered. A general trafficking role cannot settle this developmental assignment. |
| GO:0003016 respiratory system process | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific respiratory system process assertion requires its unresolved source context. Reason: The pallid mouse is a pulmonary-emphysema model, but the precise physiological experiment underlying this respiratory-process annotation remains unverified. |
| GO:0005515 protein binding | IPI PMID:12191018 Pallidin is a component of a multi-protein complex involved ... | MODIFY | Summary: The source-listed association with STX12 (Q86Y82) can be expressed as syntaxin binding. Reason: Q86Y82 is human syntaxin-12, not a BLOC-1 subunit. The curated IPI pair and the reviewed human UniProt subunit record corroborate this association; the original study is cached only as an abstract and its pair-level experiment was not independently inspected. Refine the existing interaction to the verified partner class. This does not assert a newly mapped isolated pallidin interface or transfer syntaxin catalytic or fusion activity to pallidin. Proposed replacements: syntaxin binding |
| GO:0005515 protein binding | IPI PMID:12191018 Pallidin is a component of a multi-protein complex involved ... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q8TDH9. Reason: The cached human pallidin abstract establishes a heterooligomer containing Muted; the reviewed UniProt entry also records the source interaction. The exact pair-level experiments were not independently read. Preserve the curated IPI interaction as non-core without claiming an isolated interface from the abstract. |
| GO:0005515 protein binding | IPI PMID:15102850 Identification of snapin and three novel proteins (BLOS1, BL... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:P78537. Reason: The cached abstract describes endogenous BLOC-1 co-immunoprecipitation/co-fractionation and an eight-subunit two-hybrid network. These support the curated physical association. The exact pair matrix was not independently inspected; retain generic binding as non-core rather than reject an experimental assertion from an incomplete cache. |
| GO:0005515 protein binding | IPI PMID:15102850 Identification of snapin and three novel proteins (BLOS1, BL... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q96EV8. Reason: The cached abstract describes endogenous BLOC-1 co-immunoprecipitation/co-fractionation and an eight-subunit two-hybrid network. These support the curated physical association. The exact pair matrix was not independently inspected; retain generic binding as non-core rather than reject an experimental assertion from an incomplete cache. |
| GO:0005515 protein binding | IPI PMID:15102850 Identification of snapin and three novel proteins (BLOS1, BL... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9NUP1. Reason: The cached abstract describes endogenous BLOC-1 co-immunoprecipitation/co-fractionation and an eight-subunit two-hybrid network. These support the curated physical association. The exact pair matrix was not independently inspected; retain generic binding as non-core rather than reject an experimental assertion from an incomplete cache. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q8IYI6. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q8N302. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q96BD8. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9H8W4. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9Y3C0. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:19546860 The dysbindin-containing complex (BLOC-1) in brain: developm... | MODIFY | Summary: The source-listed association with bovine SNAP47 (A6QP11) can be expressed as SNARE binding. Reason: Selected PMID:19546860 Methods and Results test native BLOC-1 from bovine brain cytosol by anti-pallidin detection in recombinant SNARE pull-downs. The source-listed partner, bovine SNAP47 (A6QP11), belongs to the SNAP SNARE class. Refine the generic interaction to SNARE binding while preserving the original partner and isoform. The measured association is with the pallidin-containing complex; it does not identify pallidin as the isolated contact surface, confer SNARE receptor activity, or establish a regulatory direction for fusion. Proposed replacements: SNARE binding |
| GO:0005515 protein binding | IPI PMID:19546860 The dysbindin-containing complex (BLOC-1) in brain: developm... | MODIFY | Summary: The source-listed association with bovine STX12 (A7MAZ2) can be expressed as syntaxin binding. Reason: Selected PMID:19546860 Methods and Results test native BLOC-1 from bovine brain cytosol by anti-pallidin detection in recombinant SNARE pull-downs. The source-listed partner is syntaxin-12/13. The experiments distinguish binding to its open SN fragment from the poorly binding complete cytoplasmic region and distinguish free SNAREs from assembled bundles. Refine this association to syntaxin binding; neither isolated-pallidin contact nor equal recognition of all syntaxins is claimed. The bovine accession-to-STX12 mapping was checked in indexed Bgee gene cross-references; the direct UniProt entry was inaccessible. Proposed replacements: syntaxin binding |
| GO:0005515 protein binding | IPI PMID:19546860 The dysbindin-containing complex (BLOC-1) in brain: developm... | MODIFY | Summary: The source-listed association with mouse SNAP25 isoform 1 (P60879-1) can be expressed as SNARE binding. Reason: Selected PMID:19546860 Methods and Results test native BLOC-1 from bovine brain cytosol by anti-pallidin detection in recombinant SNARE pull-downs. The source-listed partner, mouse SNAP25 isoform 1 (P60879-1), belongs to the SNAP SNARE class. Refine the generic interaction to SNARE binding while preserving the original partner and isoform. The measured association is with the pallidin-containing complex; it does not identify pallidin as the isolated contact surface, confer SNARE receptor activity, or establish a regulatory direction for fusion. Proposed replacements: SNARE binding |
| GO:0005515 protein binding | IPI PMID:19546860 The dysbindin-containing complex (BLOC-1) in brain: developm... | MODIFY | Summary: The source-listed association with human SNAP25 isoform 1 (P60880-1) can be expressed as SNARE binding. Reason: Selected PMID:19546860 Methods and Results test native BLOC-1 from bovine brain cytosol by anti-pallidin detection in recombinant SNARE pull-downs. The source-listed partner, human SNAP25 isoform 1 (P60880-1), belongs to the SNAP SNARE class. Refine the generic interaction to SNARE binding while preserving the original partner and isoform. The measured association is with the pallidin-containing complex; it does not identify pallidin as the isolated contact surface, confer SNARE receptor activity, or establish a regulatory direction for fusion. Proposed replacements: SNARE binding |
| GO:0005515 protein binding | IPI PMID:19546860 The dysbindin-containing complex (BLOC-1) in brain: developm... | MODIFY | Summary: The source-listed association with human SNAP25 isoform 2 (P60880-2) can be expressed as SNARE binding. Reason: Selected PMID:19546860 Methods and Results test native BLOC-1 from bovine brain cytosol by anti-pallidin detection in recombinant SNARE pull-downs. The source-listed partner, human SNAP25 isoform 2 (P60880-2), belongs to the SNAP SNARE class. Refine the generic interaction to SNARE binding while preserving the original partner and isoform. The measured association is with the pallidin-containing complex; it does not identify pallidin as the isolated contact surface, confer SNARE receptor activity, or establish a regulatory direction for fusion. Proposed replacements: SNARE binding |
| GO:0005515 protein binding | IPI PMID:19546860 The dysbindin-containing complex (BLOC-1) in brain: developm... | MODIFY | Summary: The source-listed association with human SNAP47 (Q5SQN1) can be expressed as SNARE binding. Reason: Selected PMID:19546860 Methods and Results test native BLOC-1 from bovine brain cytosol by anti-pallidin detection in recombinant SNARE pull-downs. The source-listed partner, human SNAP47 (Q5SQN1), belongs to the SNAP SNARE class. Refine the generic interaction to SNARE binding while preserving the original partner and isoform. The measured association is with the pallidin-containing complex; it does not identify pallidin as the isolated contact surface, confer SNARE receptor activity, or establish a regulatory direction for fusion. Proposed replacements: SNARE binding |
| GO:0005515 protein binding | IPI PMID:19546860 The dysbindin-containing complex (BLOC-1) in brain: developm... | MODIFY | Summary: The source-listed association with human STX12 (Q86Y82) can be expressed as syntaxin binding. Reason: Selected PMID:19546860 Methods and Results test native BLOC-1 from bovine brain cytosol by anti-pallidin detection in recombinant SNARE pull-downs. The source-listed partner is syntaxin-12/13. The experiments distinguish binding to its open SN fragment from the poorly binding complete cytoplasmic region and distinguish free SNAREs from assembled bundles. Refine this association to syntaxin binding; neither isolated-pallidin contact nor equal recognition of all syntaxins is claimed. The human Q86Y82-to-STX12 identity was checked in official NCBI and GO gene-product records. Proposed replacements: syntaxin binding |
| GO:0005515 protein binding | IPI PMID:21998198 The schizophrenia susceptibility factor dysbindin and its as... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q8R015. Reason: Selected human SH-SY5Y complex experiments recover endogenous pallidin with tagged BLOC-1 components and cargo-sorting machinery. This substantiates assembly-level physical association, not necessarily a purified binary interface. Retain the curated source association as non-core. |
| GO:0005515 protein binding | IPI PMID:22203680 Assembly and architecture of biogenesis of lysosome-related ... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:P78537. Reason: The selected human recombinant study directly reconstitutes pallidin-BLOS1 and pallidin-Cappuccino pairs and a stable ternary assembly; dysbindin is in the complete octamer. Retain the original partner-specific association as non-core, distinguishing those isolated interfaces from whole-complex membership. |
| GO:0005515 protein binding | IPI PMID:22203680 Assembly and architecture of biogenesis of lysosome-related ... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q96EV8. Reason: The selected human recombinant study directly reconstitutes pallidin-BLOS1 and pallidin-Cappuccino pairs and a stable ternary assembly; dysbindin is in the complete octamer. Retain the original partner-specific association as non-core, distinguishing those isolated interfaces from whole-complex membership. |
| GO:0005515 protein binding | IPI PMID:22203680 Assembly and architecture of biogenesis of lysosome-related ... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9NUP1. Reason: The selected human recombinant study directly reconstitutes pallidin-BLOS1 and pallidin-Cappuccino pairs and a stable ternary assembly; dysbindin is in the complete octamer. Retain the original partner-specific association as non-core, distinguishing those isolated interfaces from whole-complex membership. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:A1A4E9. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:A1L190. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: The source-listed association with STX11 (O75558) can be expressed as syntaxin binding. Reason: The original curated IPI row names O75558, which the reviewed human UniProt record identifies as STX11 and lists as a pallidin interaction. The exact source-specific supplementary pair was not independently inspected. Refine the existing association to syntaxin binding using the verified partner identity, without assigning a physiological vesicle route, isolated binding site, or syntaxin enzymatic activity to pallidin. Proposed replacements: syntaxin binding |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:P37198. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:P78537. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q13503. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q13561. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q16637. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q5VU62. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q6QEF8. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q8N619. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q8TD31-3. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q96BD8. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q96CS2. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q96JN2-2. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9NYB9. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9UJ41. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:29892012 An interactome perturbation framework prioritizes damaging m... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9NYB9. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q96BD8. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9Y3C0. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The source-listed association with STX11 (O75558) can be expressed as syntaxin binding. Reason: The original curated IPI row names O75558, which the reviewed human UniProt record identifies as STX11 and lists as a pallidin interaction. The exact source-specific supplementary pair was not independently inspected. Refine the existing association to syntaxin binding using the verified partner identity, without assigning a physiological vesicle route, isolated binding site, or syntaxin enzymatic activity to pallidin. Proposed replacements: syntaxin binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:P09493-10. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:P37198. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:P78537. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q14CN4. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The source-listed association with STX1A (Q16623) can be expressed as syntaxin-1 binding. Reason: The original curated IPI pair names Q16623, identified as human STX1A in the reviewed UniProt interaction record. The official GO definition of syntaxin-1 binding matches this partner more precisely than generic protein binding. The exact supplementary pair-level experiment was not independently inspected; retain that limit and do not infer a native synaptic mechanism merely from this interaction. Proposed replacements: syntaxin-1 binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q16637. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q2T9L4. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q504U0. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q6NUQ1. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q8IY31-3. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q8IYI6. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q96BD8. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q96EV8. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9BV36. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9C0F1. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9H8W4. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9NYB9-2. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9UJ41-4. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9Y3C0. Reason: The cached abstract establishes a systematic human interaction or variant-perturbation study. The exact pair-level supplementary experiment was not independently inspected. Preserve this curated experimental interaction as non-core, with its original partner identifier, rather than infer the partner's biological function or reject it from abstract-only evidence. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:P78537. Reason: BioPlex affinity-purification mass spectrometry maps physical associations in human cell lines. The source record is retained as non-core; the pair-level supplementary dataset was not independently inspected, and co-purification does not by itself establish a direct binary interface. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q8N302. Reason: BioPlex affinity-purification mass spectrometry maps physical associations in human cell lines. The source record is retained as non-core; the pair-level supplementary dataset was not independently inspected, and co-purification does not by itself establish a direct binary interface. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q96BD8. Reason: BioPlex affinity-purification mass spectrometry maps physical associations in human cell lines. The source record is retained as non-core; the pair-level supplementary dataset was not independently inspected, and co-purification does not by itself establish a direct binary interface. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q96EV8. Reason: BioPlex affinity-purification mass spectrometry maps physical associations in human cell lines. The source record is retained as non-core; the pair-level supplementary dataset was not independently inspected, and co-purification does not by itself establish a direct binary interface. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9C0F1. Reason: BioPlex affinity-purification mass spectrometry maps physical associations in human cell lines. The source record is retained as non-core; the pair-level supplementary dataset was not independently inspected, and co-purification does not by itself establish a direct binary interface. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9NUP1. Reason: BioPlex affinity-purification mass spectrometry maps physical associations in human cell lines. The source record is retained as non-core; the pair-level supplementary dataset was not independently inspected, and co-purification does not by itself establish a direct binary interface. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q9Y3C0. Reason: BioPlex affinity-purification mass spectrometry maps physical associations in human cell lines. The source record is retained as non-core; the pair-level supplementary dataset was not independently inspected, and co-purification does not by itself establish a direct binary interface. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: Pallidin physically associates with UniProtKB:Q96EV8. Reason: The cached abstract establishes the multimodal human cell-map context. The curated pallidin-dysbindin association agrees with BLOC-1 membership; the pair-level data were not independently reanalyzed. The official correction changes a duplicated loss-function equation and does not identify a change to this interaction. Retain the physical association as non-core. |
| GO:0005737 cytoplasm | IDA PMID:12019270 BLOC-1, a novel complex containing the pallidin and muted pr... | ACCEPT | Summary: Pallidin has a cytoplasmic pool. Reason: Human pallidin biochemical fractionation and the reviewed UniProt record establish a soluble cytoplasmic pool together with peripheral membrane association. This broad location is consistent with the BLOC-1 trafficking role. Supporting Evidence: PMID:12019270 Endogenous pallidin was distributed in both soluble and peripheral membrane protein fractions. UniProt:Q9UL45 |
| GO:0005737 cytoplasm | IDA PMID:12191018 Pallidin is a component of a multi-protein complex involved ... | ACCEPT | Summary: Pallidin has a cytoplasmic pool. Reason: Human pallidin biochemical fractionation and the reviewed UniProt record establish a soluble cytoplasmic pool together with peripheral membrane association. This broad location is consistent with the BLOC-1 trafficking role. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: Pallidin has a cytoplasmic pool. Reason: Human pallidin biochemical fractionation and the reviewed UniProt record establish a soluble cytoplasmic pool together with peripheral membrane association. This broad location is consistent with the BLOC-1 trafficking role. |
| GO:0005768 endosome | IEA GO_REF:0000107 | ACCEPT | Summary: Pallidin-containing BLOC-1 acts at endosomal membranes. Reason: Human PaHA complementation in pallid mouse melanocytes restores Tyrp1 sorting from early endosomes toward melanosomes; selected endogenous-complex work independently supports membrane association. Retain the mouse-derived endosomal assignment without implying an intraluminal topology. |
| GO:0005788 endoplasmic reticulum lumen | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: ER-lumen localization overstates the established topology of pallidin. Reason: The ER lumen is separated from cytosolic BLOC-1 by the ER membrane. Human pallidin is characterized as a cytoplasmic, peripheral-membrane coiled-coil subunit, with no annotated signal peptide or membrane-spanning segment. A lumen assignment therefore extends beyond the supported compartment and topology. Mark this electronic transfer as over-annotated without asserting that its unresolved mouse source is experimentally false or that all unconventional import routes are impossible. The established cytoplasmic and membrane-associated assertions are retained; no replacement location is invented. |
| GO:0005829 cytosol | IEA GO_REF:0000107 | ACCEPT | Summary: Pallidin is a cytosolic BLOC-1 subunit. Reason: The cytosolic biochemical pool is directly supported by human pallidin studies. Reactome R-HSA-429815 describes formation of the eight-component BLOC-1 assembly; the independent fractionation evidence supplies the localization support rather than relying on an event title alone. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-429815 | ACCEPT | Summary: Pallidin is a cytosolic BLOC-1 subunit. Reason: The cytosolic biochemical pool is directly supported by human pallidin studies. Reactome R-HSA-429815 describes formation of the eight-component BLOC-1 assembly; the independent fractionation evidence supplies the localization support rather than relying on an event title alone. |
| GO:0005884 actin filament | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Pallidin-containing material associates with filamentous actin. Reason: Selected PMID:12019270 methods and results show pallidin-containing cytosolic material sedimenting with purified F-actin and tagged human pallidin at perinuclear actin structures. The authors explicitly leave direct binding versus mediation by other actin-associated proteins unresolved. Preserve the experimental and transferred association as non-core without assigning pallidin an actin-polymerizing or crosslinking mechanism; the filamentous-actin part_of assertion is read as association, not incorporation as an actin monomer. Supporting Evidence: |
| GO:0005925 focal adhesion | IBA GO_REF:0000033 | UNDECIDED | Summary: The specific focal adhesion assertion requires its unresolved source context. Reason: The exact mouse focal-adhesion experiment and the PAINT node placement were not reconstructed. BLOC-1 membership and F-actin association do not by themselves establish this localization; no donor-count or name-confusion argument is used. |
| GO:0005925 focal adhesion | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific focal adhesion assertion requires its unresolved source context. Reason: The actual mouse focal-adhesion localization assay remains unverified. Perinuclear F-actin association is a different localization and neither confirms nor refutes the donor experiment. |
| GO:0006520 amino acid metabolic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Altered metabolite abundance does not establish direct participation of pallidin in amino acid metabolic process. Reason: PMID:28701731 compares postnatal day 1–2 pallid and control mouse hippocampi by untargeted metabolomics and reports altered metabolite pools and increased SNAT1 abundance. The selected Results, Table 1, Discussion and Methods support a downstream metabolic consequence of BLOC-1 deficiency; they do not demonstrate pallidin performing a reaction or supplying a metabolic scaffold or cofactor. This distinction concerns participation in the named metabolic process, not merely absence of catalytic activity. The exact current mouse donor GO-row/reference edge remains unresolved, so this study is independent corroboration rather than a claimed reconstruction of that transfer. Supporting Evidence: |
| GO:0006531 aspartate metabolic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Altered metabolite abundance does not establish direct participation of pallidin in aspartate metabolic process. Reason: PMID:28701731 compares postnatal day 1–2 pallid and control mouse hippocampi by untargeted metabolomics and reports altered metabolite pools and increased SNAT1 abundance. The selected Results, Table 1, Discussion and Methods support a downstream metabolic consequence of BLOC-1 deficiency; they do not demonstrate pallidin performing a reaction or supplying a metabolic scaffold or cofactor. This distinction concerns participation in the named metabolic process, not merely absence of catalytic activity. The exact current mouse donor GO-row/reference edge remains unresolved, so this study is independent corroboration rather than a claimed reconstruction of that transfer. Supporting Evidence: |
| GO:0006536 glutamate metabolic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Altered metabolite abundance does not establish direct participation of pallidin in glutamate metabolic process. Reason: PMID:28701731 compares postnatal day 1–2 pallid and control mouse hippocampi by untargeted metabolomics and reports altered metabolite pools and increased SNAT1 abundance. The selected Results, Table 1, Discussion and Methods support a downstream metabolic consequence of BLOC-1 deficiency; they do not demonstrate pallidin performing a reaction or supplying a metabolic scaffold or cofactor. This distinction concerns participation in the named metabolic process, not merely absence of catalytic activity. The exact current mouse donor GO-row/reference edge remains unresolved, so this study is independent corroboration rather than a claimed reconstruction of that transfer. Supporting Evidence: |
| GO:0006541 L-glutamine metabolic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Altered metabolite abundance does not establish direct participation of pallidin in L-glutamine metabolic process. Reason: PMID:28701731 compares postnatal day 1–2 pallid and control mouse hippocampi by untargeted metabolomics and reports altered metabolite pools and increased SNAT1 abundance. The selected Results, Table 1, Discussion and Methods support a downstream metabolic consequence of BLOC-1 deficiency; they do not demonstrate pallidin performing a reaction or supplying a metabolic scaffold or cofactor. This distinction concerns participation in the named metabolic process, not merely absence of catalytic activity. The exact current mouse donor GO-row/reference edge remains unresolved, so this study is independent corroboration rather than a claimed reconstruction of that transfer. Supporting Evidence: |
| GO:0006644 phospholipid metabolic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Altered metabolite abundance does not establish direct participation of pallidin in phospholipid metabolic process. Reason: PMID:28701731 compares postnatal day 1–2 pallid and control mouse hippocampi by untargeted metabolomics and reports altered metabolite pools and increased SNAT1 abundance. The selected Results, Table 1, Discussion and Methods support a downstream metabolic consequence of BLOC-1 deficiency; they do not demonstrate pallidin performing a reaction or supplying a metabolic scaffold or cofactor. This distinction concerns participation in the named metabolic process, not merely absence of catalytic activity. The exact current mouse donor GO-row/reference edge remains unresolved, so this study is independent corroboration rather than a claimed reconstruction of that transfer. Supporting Evidence: |
| GO:0006954 inflammatory response | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Pallidin deficiency affects inflammatory neutrophil function and host defense in mice. Reason: Independently inspected primary PMID:17785837 experiments show impaired elastase release by pallid mouse inflammatory neutrophils, reduced support of parasite killing by infected macrophages, and impaired parasite control after neutrophil transfer. These support a non-core physiological consequence of BLOC-1-dependent granule release. Pallidin is not the assayed protease, immune receptor or oxidant-generating enzyme. The current mouse GO-row/reference edge remains unresolved; this study is independent corroboration, not a claimed reconstruction of the transfer. Supporting Evidence: |
| GO:0006955 immune response | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Pallidin deficiency affects inflammatory neutrophil function and host defense in mice. Reason: Independently inspected primary PMID:17785837 experiments show impaired elastase release by pallid mouse inflammatory neutrophils, reduced support of parasite killing by infected macrophages, and impaired parasite control after neutrophil transfer. These support a non-core physiological consequence of BLOC-1-dependent granule release. Pallidin is not the assayed protease, immune receptor or oxidant-generating enzyme. The current mouse GO-row/reference edge remains unresolved; this study is independent corroboration, not a claimed reconstruction of the transfer. Supporting Evidence: |
| GO:0006979 response to oxidative stress | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific response to oxidative stress assertion requires its unresolved source context. Reason: Positive redox evidence exists: selected primary PMID:22423091 results and Figure 7 caption describe increased basal oxidant signal and reduced peroxiredoxins after pallidin shRNA in human SH-SY5Y cells. Basal oxidant accumulation following protein loss does not alone establish the specific response-to-oxidative-stress process or pallidin peroxidase chemistry. The exact mouse donor-source edge and term fit remain unresolved, so retain UNDECIDED without denying that phenotype. Supporting Evidence: |
| GO:0007010 cytoskeleton organization | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific cytoskeleton organization assertion requires its unresolved source context. Reason: Association with F-actin and the primary neurite phenotype do not isolate a pallidin-dependent cytoskeletal-organization step. The source mouse organization assay remains unverified. Supporting Evidence: |
| GO:0007032 endosome organization | IEA GO_REF:0000107 | ACCEPT | Summary: BLOC-1 supports endosomal organization and cargo sorting. Reason: Pallid melanocytes show altered Tyrp1 routing and endosomal cargo distribution, with restoration by human PaHA. This establishes a contribution of the pallidin-containing assembly to the endosomal pathway. The 2017 correction revises the transferrin control to a mild early recycling defect; it does not erase the independently supported Tyrp1 result. |
| GO:0007613 memory | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific memory assertion requires its unresolved source context. Reason: The inspected neonatal hippocampal and neurite studies do not establish the exact adult learning or memory assay used by the donor annotation. |
| GO:0008021 synaptic vesicle | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific synaptic vesicle assertion requires its unresolved source context. Reason: The inspected neuronal experiments concern BLOC-1-associated cargo and small intracellular vesicle fractions. They do not independently resolve pallidin itself on mature synaptic vesicles; the exact donor localization remains unverified. |
| GO:0008089 anterograde axonal transport | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BLOC-1 supports delivery of selected neuronal membrane cargo. Reason: Selected PMID:21998198 experiments include pallid mouse fibroblasts and dentate-gyrus cargo distribution, together with human neuronal-cell complexes containing endogenous pallidin. These support the neuronal trafficking pathway and the curator-mediated orthology inferences, rather than pallidin acting as an axonal motor or transporting every mature synaptic vesicle. Keep this neuronal specialization as non-core. |
| GO:0008089 anterograde axonal transport | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: BLOC-1 supports delivery of selected neuronal membrane cargo. Reason: Selected PMID:21998198 experiments include pallid mouse fibroblasts and dentate-gyrus cargo distribution, together with human neuronal-cell complexes containing endogenous pallidin. These support the neuronal trafficking pathway and the curator-mediated orthology inferences, rather than pallidin acting as an axonal motor or transporting every mature synaptic vesicle. Keep this neuronal specialization as non-core. |
| GO:0009306 protein secretion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Pallidin supports granule-protein release in a trafficking-dependent physiological context. Reason: PMID:17785837 directly measures reduced elastase release from living pallid mouse inflammatory neutrophils. Human patient NK-cell experiments in the independently identified 2012 PMID:22461475 also show impaired degranulation, abnormal lysosomal-marker distribution and correction of CD107a distribution by PLDN replacement. Together with pallidin’s role in BLOC-1 trafficking machinery, these observations support retaining this existing secretion annotation as non-core. Pallidin contributes trafficking machinery; it is neither the secreted elastase substrate nor its protease. The specific molecular step in neutrophil release and the exact current donor GO-row/reference edge remain unresolved. |
| GO:0010467 gene expression | IEA GO_REF:0000107 | UNDECIDED | Summary: The functional basis of the transferred gene-expression assertion remains unresolved. Reason: The current mouse experiment underlying this electronic transfer has not been identified. Pallidin has an established BLOC-1 trafficking role, but that fact alone cannot exclude every additional activity in RNA or protein expression. Changed downstream abundance would not by itself demonstrate participation; it has not been established that such a measurement was the sole basis of this donor annotation. Retain UNDECIDED for the missing source context instead of treating a hypothetical experiment as an inspected refutation. |
| GO:0014823 response to activity | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific response to activity assertion requires its unresolved source context. Reason: The precise activity-response experiment in the mouse donor is unresolved. The fly high-activity recycling result is useful context but cannot reconstruct this particular transfer. |
| GO:0016020 membrane | EXP PMID:12019270 BLOC-1, a novel complex containing the pallidin and muted pr... | ACCEPT | Summary: Pallidin associates peripherally with membranes. Reason: Human pallidin occurs in soluble and membrane-associated fractions, and the inspected studies characterize its membrane pool as peripheral. Retain the broad membrane location without turning this non-transmembrane BLOC-1 subunit into a membrane-spanning transporter. |
| GO:0016020 membrane | EXP PMID:12191018 Pallidin is a component of a multi-protein complex involved ... | ACCEPT | Summary: Pallidin associates peripherally with membranes. Reason: Human pallidin occurs in soluble and membrane-associated fractions, and the inspected studies characterize its membrane pool as peripheral. Retain the broad membrane location without turning this non-transmembrane BLOC-1 subunit into a membrane-spanning transporter. |
| GO:0016020 membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Pallidin associates peripherally with membranes. Reason: Human pallidin occurs in soluble and membrane-associated fractions, and the inspected studies characterize its membrane pool as peripheral. Retain the broad membrane location without turning this non-transmembrane BLOC-1 subunit into a membrane-spanning transporter. |
| GO:0016197 endosomal transport | IEA GO_REF:0000107 | ACCEPT | Summary: BLOC-1 supports endosomal organization and cargo sorting. Reason: Pallid melanocytes show altered Tyrp1 routing and endosomal cargo distribution, with restoration by human PaHA. This establishes a contribution of the pallidin-containing assembly to the endosomal pathway. The 2017 correction revises the transferrin control to a mild early recycling defect; it does not erase the independently supported Tyrp1 result. |
| GO:0019905 syntaxin binding | TAS PMID:10610180 The pallid gene encodes a novel, syntaxin 13-interacting pro... | ACCEPT | Summary: Pallidin associates with syntaxin trafficking machinery. Reason: The complete normal abstract of PMID:10610180 reports a syntaxin-13 interaction identified by two-hybrid analysis and confirmed by co-immunoprecipitation. This is the original curated TAS source, alongside the human UniProt interaction record. Later native brain BLOC-1 experiments distinguish open syntaxin binding from closed or assembled SNARE states; they do not imply binding to every syntaxin. |
| GO:0021542 dentate gyrus development | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific dentate gyrus development assertion requires its unresolved source context. Reason: Dentate-gyrus cargo distribution is measured in pallid mice, but that is not itself a developmental assay of formation of the dentate gyrus. The exact developmental evidence remains unverified. |
| GO:0021854 hypothalamus development | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific hypothalamus development assertion requires its unresolved source context. Reason: The selected neuronal trafficking evidence does not resolve hypothalamus development; its specific mouse donor experiment remains unverified. |
| GO:0030133 transport vesicle | IBA GO_REF:0000033 | UNDECIDED | Summary: The specific transport vesicle assertion requires its unresolved source context. Reason: The target self-entry in the IBA is legitimate experimental grounding, not circularity. The inspected localization passage in PMID:17182842 resolves MuHA-reconstituted BLOC-1 on tubulovesicular endosomes; it does not separately map pallidin there. The exact pallidin carrier-localization basis, including uninspected supplementary material and PAINT placement, remains unresolved. Supporting Evidence: |
| GO:0030133 transport vesicle | IDA PMID:17182842 BLOC-1 is required for cargo-specific sorting from vacuolar ... | UNDECIDED | Summary: The specific transport vesicle assertion requires its unresolved source context. Reason: Selected PMID:17182842 body text establishes human PaHA rescue and separately maps MuHA-reconstituted BLOC-1 on tubulovesicular endosomes. The exact pallidin-specific localization assay or supplementary image underlying this IDA was not independently resolved; preserve the experimental assertion as undecided instead of rejecting it from incomplete coverage. Supporting Evidence: |
| GO:0030324 lung development | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific lung development assertion requires its unresolved source context. Reason: The exact mouse lung-development assay remains unverified. Pulmonary pathology does not by itself identify a developmental rather than maintenance defect. |
| GO:0031083 BLOC-1 complex | IBA GO_REF:0000033 | ACCEPT | Summary: Pallidin is an integral BLOC-1 complex subunit. Reason: Human biochemical studies and complete recombinant octamer reconstitution establish pallidin membership. Pallidin, Cappuccino and BLOS1 form a stable subassembly. The IBA target self-entry represents legitimate descendant experimental grounding, not circular evidence; the full PAINT ancestral placement was not independently reconstructed. |
| GO:0031083 BLOC-1 complex | IDA PMID:12019270 BLOC-1, a novel complex containing the pallidin and muted pr... | ACCEPT | Summary: Pallidin is an integral BLOC-1 complex subunit. Reason: Human biochemical studies and complete recombinant octamer reconstitution establish pallidin membership. Pallidin, Cappuccino and BLOS1 form a stable subassembly. The IBA target self-entry represents legitimate descendant experimental grounding, not circular evidence; the full PAINT ancestral placement was not independently reconstructed. |
| GO:0031083 BLOC-1 complex | IDA PMID:15102850 Identification of snapin and three novel proteins (BLOS1, BL... | ACCEPT | Summary: Pallidin is an integral BLOC-1 complex subunit. Reason: Human biochemical studies and complete recombinant octamer reconstitution establish pallidin membership. Pallidin, Cappuccino and BLOS1 form a stable subassembly. The IBA target self-entry represents legitimate descendant experimental grounding, not circular evidence; the full PAINT ancestral placement was not independently reconstructed. |
| GO:0031083 BLOC-1 complex | IDA PMID:17182842 BLOC-1 is required for cargo-specific sorting from vacuolar ... | ACCEPT | Summary: Pallidin is an integral BLOC-1 complex subunit. Reason: Human biochemical studies and complete recombinant octamer reconstitution establish pallidin membership. Pallidin, Cappuccino and BLOS1 form a stable subassembly. The IBA target self-entry represents legitimate descendant experimental grounding, not circular evidence; the full PAINT ancestral placement was not independently reconstructed. |
| GO:0031083 BLOC-1 complex | IDA PMID:22203680 Assembly and architecture of biogenesis of lysosome-related ... | ACCEPT | Summary: Pallidin is an integral BLOC-1 complex subunit. Reason: Human biochemical studies and complete recombinant octamer reconstitution establish pallidin membership. Pallidin, Cappuccino and BLOS1 form a stable subassembly. The IBA target self-entry represents legitimate descendant experimental grounding, not circular evidence; the full PAINT ancestral placement was not independently reconstructed. |
| GO:0031083 BLOC-1 complex | IEA GO_REF:0000107 | ACCEPT | Summary: Pallidin is an integral BLOC-1 complex subunit. Reason: Human biochemical studies and complete recombinant octamer reconstitution establish pallidin membership. Pallidin, Cappuccino and BLOS1 form a stable subassembly. The IBA target self-entry represents legitimate descendant experimental grounding, not circular evidence; the full PAINT ancestral placement was not independently reconstructed. |
| GO:0031083 BLOC-1 complex | IPI PMID:22203680 Assembly and architecture of biogenesis of lysosome-related ... | ACCEPT | Summary: Pallidin is an integral BLOC-1 complex subunit. Reason: Human biochemical studies and complete recombinant octamer reconstitution establish pallidin membership. Pallidin, Cappuccino and BLOS1 form a stable subassembly. The IBA target self-entry represents legitimate descendant experimental grounding, not circular evidence; the full PAINT ancestral placement was not independently reconstructed. |
| GO:0031175 neuron projection development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Pallidin deficiency affects neurite development. Reason: PMID:19546860 directly compares primary pallid and control mouse hippocampal neurons and finds modest reductions in neurite number and total length. This is target-relevant experimental evidence despite the title foregrounding dysbindin. Retain the human orthology-based developmental annotation as non-core, without claiming a separately demonstrated human neuron mechanism. Supporting Evidence: |
| GO:0031175 neuron projection development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Pallidin deficiency affects neurite development. Reason: PMID:19546860 directly compares primary pallid and control mouse hippocampal neurons and finds modest reductions in neurite number and total length. This is target-relevant experimental evidence despite the title foregrounding dysbindin. Retain the human orthology-based developmental annotation as non-core, without claiming a separately demonstrated human neuron mechanism. Supporting Evidence: |
| GO:0031410 cytoplasmic vesicle | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: BLOC-1 associates with cytoplasmic vesicular trafficking compartments. Reason: The ARBA assignment is broadly consistent with the peripheral membrane pool and endosomal trafficking function of pallidin-containing BLOC-1. Retain this broad inferred location as non-core; it is not a separately resolved pallidin localization experiment for every vesicle class. |
| GO:0031941 filamentous actin | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Pallidin-containing material associates with filamentous actin. Reason: Selected PMID:12019270 methods and results show pallidin-containing cytosolic material sedimenting with purified F-actin and tagged human pallidin at perinuclear actin structures. The authors explicitly leave direct binding versus mediation by other actin-associated proteins unresolved. Preserve the experimental and transferred association as non-core without assigning pallidin an actin-polymerizing or crosslinking mechanism; the filamentous-actin part_of assertion is read as association, not incorporation as an actin monomer. Supporting Evidence: |
| GO:0032400 melanosome localization | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific melanosome localization assertion requires its unresolved source context. Reason: The inspected human PaHA rescue establishes cargo delivery and pigmentation, not the positioning of whole melanosomes. The specific mouse organelle-localization experiment remains unverified. Supporting Evidence: |
| GO:0032402 melanosome transport | IBA GO_REF:0000033 | UNDECIDED | Summary: Whole-melanosome movement is not resolved by the inspected cargo-routing experiments. Reason: GO:0032402 describes directed movement of whole melanosomes; inspected pallidin rescue experiments measure Tyrp1 cargo delivery to melanosomes, already represented by GO:0035646. The target self-entry is valid descendant evidence, not circularity. Neither the complete PAINT ancestral placement nor the entire experimental basis for whole-organelle movement was inspected. Retain UNDECIDED; do not replace this assertion with a duplicate cargo term or infer that the curator’s complete evidence contained no movement assay. Supporting Evidence: |
| GO:0032402 melanosome transport | IDA PMID:17182842 BLOC-1 is required for cargo-specific sorting from vacuolar ... | UNDECIDED | Summary: Whole-melanosome movement is not resolved by the inspected pallidin rescue experiment. Reason: Selected PMID:17182842 Methods, Results and Discussion establish restoration of Tyrp1 cargo routing and pigmentation in pallid melanocytes complemented with human pallidin. These endpoints do not by themselves measure directed movement of whole melanosomes. Complete figure images and supplementary material were not inspected, leaving the experimental IDA assertion unresolved. Retain UNDECIDED rather than remove it from incomplete evidence or duplicate the separately accepted cargo-delivery annotation. Supporting Evidence: |
| GO:0032438 melanosome organization | NAS PMID:15102850 Identification of snapin and three novel proteins (BLOS1, BL... | ACCEPT | Summary: Pallidin-containing BLOC-1 supports melanosome organization. Reason: Complex assembly and human PaHA rescue of pallid melanocytes support melanosome biogenesis through delivery of membrane cargo. The retained NAS annotations are consistent with this mechanism and do not assert that pallidin synthesizes pigment or moves whole organelles. |
| GO:0032438 melanosome organization | NAS PMID:22203680 Assembly and architecture of biogenesis of lysosome-related ... | ACCEPT | Summary: Pallidin-containing BLOC-1 supports melanosome organization. Reason: Complex assembly and human PaHA rescue of pallid melanocytes support melanosome biogenesis through delivery of membrane cargo. The retained NAS annotations are consistent with this mechanism and do not assert that pallidin synthesizes pigment or moves whole organelles. |
| GO:0035264 multicellular organism growth | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific multicellular organism growth assertion requires its unresolved source context. Reason: The exact mouse organismal-growth assay remains unverified. Early neuronal and pigment phenotypes do not settle a whole-organism growth mechanism. |
| GO:0035641 locomotory exploration behavior | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific locomotory exploration behavior assertion requires its unresolved source context. Reason: The precise exploratory-behavior assay in pallid mice has not been independently verified; vestibular, locomotor and cognitive endpoints are not interchangeable. |
| GO:0035646 endosome to melanosome transport | IDA PMID:17182842 BLOC-1 is required for cargo-specific sorting from vacuolar ... | ACCEPT | Summary: Pallidin supports transport of cargo from endosomes to melanosomes. Reason: Selected PMID:17182842 experiments directly compare pallid melanocytes with human PaHA rescue and measure Tyrp1 surface/endosomal accumulation versus delivery to melanosomes. This matches cargo movement between compartments. The 2017 correction invalidates the original transferrin-FITC control; corrected recycling measurements do not overturn this cargo-sorting result. Supporting Evidence: |
| GO:0035646 endosome to melanosome transport | IEA GO_REF:0000107 | ACCEPT | Summary: Pallidin supports transport of cargo from endosomes to melanosomes. Reason: Selected PMID:17182842 experiments directly compare pallid melanocytes with human PaHA rescue and measure Tyrp1 surface/endosomal accumulation versus delivery to melanosomes. This matches cargo movement between compartments. The 2017 correction invalidates the original transferrin-FITC control; corrected recycling measurements do not overturn this cargo-sorting result. Supporting Evidence: |
| GO:0035651 AP-3 adaptor complex binding | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific AP-3 adaptor complex binding assertion requires its unresolved source context. Reason: The inspected human recombinant BLOC-1 octamer binds AP-3, and pallidin-containing cell complexes associate with AP-3 machinery. Those experiments do not isolate a pallidin–AP-3 interface; the exact mouse donor binding assay remains unresolved. |
| GO:0036064 ciliary basal body | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific ciliary basal body assertion requires its unresolved source context. Reason: The specific pallidin basal-body localization experiment was not recovered. Ciliary trafficking by other BLOC-1 components cannot replace target-specific evidence. |
| GO:0036269 swimming behavior | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific swimming behavior assertion requires its unresolved source context. Reason: Pallid mice have an explicit otolith phenotype, but the precise swimming assay used for this mouse GO transfer was not independently verified. A plausible vestibular explanation does not establish the exact behavioral endpoint. |
| GO:0036466 synaptic vesicle recycling via endosome | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Pallidin supports activity-dependent synaptic-vesicle recycling in the curated ancestral context. Reason: The IBA uses Drosophila Pldn (FBgn0036192). Independently inspected official primary evidence for PMID:28317021 describes activity-dependent recycling-pool failure and endosomal abnormalities in fly pldn mutants, with relatively preserved basal transmission. Retain this neuronal specialization as non-core; the complete PAINT tree was not reanalyzed and the donor reference-to-node join was not reconstructed. No autonomous vesicle motor is implied. |
| GO:0042745 circadian sleep/wake cycle | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific circadian sleep/wake cycle assertion requires its unresolved source context. Reason: The exact mouse circadian sleep/wake experiment remains unverified. General behavioral or neurotransmitter changes cannot be substituted for a circadian measurement. |
| GO:0042802 identical protein binding | IPI PMID:15102850 Identification of snapin and three novel proteins (BLOS1, BL... | KEEP AS NON CORE | Summary: Pallidin can self-associate in the tested interaction systems. Reason: Selected PMID:12019270 experiments map human pallidin self-association to its coiled-coil-containing region, and other source interaction records retain self-binding. The complete BLOC-1 octamer has one copy of each subunit; that physiological stoichiometry does not refute isolated self-association assays. Retain these experimental observations as non-core rather than infer a pallidin homodimer as the functional BLOC-1 unit. |
| GO:0042802 identical protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | KEEP AS NON CORE | Summary: Pallidin can self-associate in the tested interaction systems. Reason: Selected PMID:12019270 experiments map human pallidin self-association to its coiled-coil-containing region, and other source interaction records retain self-binding. The complete BLOC-1 octamer has one copy of each subunit; that physiological stoichiometry does not refute isolated self-association assays. Retain these experimental observations as non-core rather than infer a pallidin homodimer as the functional BLOC-1 unit. |
| GO:0042802 identical protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Pallidin can self-associate in the tested interaction systems. Reason: Selected PMID:12019270 experiments map human pallidin self-association to its coiled-coil-containing region, and other source interaction records retain self-binding. The complete BLOC-1 octamer has one copy of each subunit; that physiological stoichiometry does not refute isolated self-association assays. Retain these experimental observations as non-core rather than infer a pallidin homodimer as the functional BLOC-1 unit. |
| GO:0042803 protein homodimerization activity | IDA PMID:12019270 BLOC-1, a novel complex containing the pallidin and muted pr... | KEEP AS NON CORE | Summary: Pallidin can self-associate in the tested interaction systems. Reason: Selected PMID:12019270 experiments map human pallidin self-association to its coiled-coil-containing region, and other source interaction records retain self-binding. The complete BLOC-1 octamer has one copy of each subunit; that physiological stoichiometry does not refute isolated self-association assays. Retain these experimental observations as non-core rather than infer a pallidin homodimer as the functional BLOC-1 unit. |
| GO:0042803 protein homodimerization activity | IDA PMID:12191018 Pallidin is a component of a multi-protein complex involved ... | KEEP AS NON CORE | Summary: Pallidin can self-associate in the tested interaction systems. Reason: Selected PMID:12019270 experiments map human pallidin self-association to its coiled-coil-containing region, and other source interaction records retain self-binding. The complete BLOC-1 octamer has one copy of each subunit; that physiological stoichiometry does not refute isolated self-association assays. Retain these experimental observations as non-core rather than infer a pallidin homodimer as the functional BLOC-1 unit. |
| GO:0043197 dendritic spine | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific dendritic spine assertion requires its unresolved source context. Reason: The inspected neonatal neurite and cargo-distribution studies do not independently establish pallidin localization at dendritic spines; the actual donor localization remains unverified. |
| GO:0043588 skin development | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific skin development assertion requires its unresolved source context. Reason: Pigment dilution and melanosomal defects are established, but these do not themselves resolve a skin-development process. The specific developmental donor assay remains unverified. |
| GO:0043679 axon terminus | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific axon terminus assertion requires its unresolved source context. Reason: Neuronal cargo reaches axonal terminals through BLOC-1-dependent routes, but cargo depletion is not itself direct localization of pallidin at the terminus. The exact mouse donor location assay remains unverified. |
| GO:0044291 cell-cell contact zone | IBA GO_REF:0000033 | UNDECIDED | Summary: The specific cell-cell contact zone assertion requires its unresolved source context. Reason: The actual mouse cell-contact localization and PAINT node evidence were not reconstructed. F-actin association and complex assembly do not settle this spatially specific term; the IBA is not discounted because of its donor count. |
| GO:0044291 cell-cell contact zone | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific cell-cell contact zone assertion requires its unresolved source context. Reason: The exact mouse cell-cell-contact localization assay remains unverified. The human cytoplasmic/perinuclear observations concern a different spatial resolution. |
| GO:0044297 cell body | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific cell body assertion requires its unresolved source context. Reason: The protein-trafficking study measures cargo distribution between neuronal cell bodies and neurites; it does not by itself locate endogenous pallidin in the exact donor context. The source localization assay remains unverified. |
| GO:0046085 adenosine metabolic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Altered metabolite abundance does not establish direct participation of pallidin in adenosine metabolic process. Reason: PMID:28701731 compares postnatal day 1–2 pallid and control mouse hippocampi by untargeted metabolomics and reports altered metabolite pools and increased SNAT1 abundance. The selected Results, Table 1, Discussion and Methods support a downstream metabolic consequence of BLOC-1 deficiency; they do not demonstrate pallidin performing a reaction or supplying a metabolic scaffold or cofactor. This distinction concerns participation in the named metabolic process, not merely absence of catalytic activity. The exact current mouse donor GO-row/reference edge remains unresolved, so this study is independent corroboration rather than a claimed reconstruction of that transfer. Supporting Evidence: |
| GO:0048066 developmental pigmentation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Pallidin deficiency alters pigmentation through organelle trafficking. Reason: Pallid mice show pigment dilution, and human PaHA restores pigmentation in established mutant melanocytes. Retain the pigmentation phenotypes inferred from the mouse ortholog as non-core consequences of melanosomal cargo delivery, without assigning pigment synthesis chemistry to pallidin. |
| GO:0048069 eye pigmentation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Pallidin deficiency alters pigmentation through organelle trafficking. Reason: Pallid mice show pigment dilution, and human PaHA restores pigmentation in established mutant melanocytes. Retain the pigmentation phenotypes inferred from the mouse ortholog as non-core consequences of melanosomal cargo delivery, without assigning pigment synthesis chemistry to pallidin. |
| GO:0048286 lung alveolus development | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific lung alveolus development assertion requires its unresolved source context. Reason: The exact mouse alveolar-development experiment remains unverified. Emphysema and alveolar maintenance phenotypes must be distinguished from developmental formation. |
| GO:0048490 anterograde synaptic vesicle transport | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BLOC-1 supports delivery of selected neuronal membrane cargo. Reason: Selected PMID:21998198 experiments include pallid mouse fibroblasts and dentate-gyrus cargo distribution, together with human neuronal-cell complexes containing endogenous pallidin. These support the neuronal trafficking pathway and the curator-mediated orthology inferences, rather than pallidin acting as an axonal motor or transporting every mature synaptic vesicle. Keep this neuronal specialization as non-core. |
| GO:0048490 anterograde synaptic vesicle transport | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: BLOC-1 supports delivery of selected neuronal membrane cargo. Reason: Selected PMID:21998198 experiments include pallid mouse fibroblasts and dentate-gyrus cargo distribution, together with human neuronal-cell complexes containing endogenous pallidin. These support the neuronal trafficking pathway and the curator-mediated orthology inferences, rather than pallidin acting as an axonal motor or transporting every mature synaptic vesicle. Keep this neuronal specialization as non-core. |
| GO:0048813 dendrite morphogenesis | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific dendrite morphogenesis assertion requires its unresolved source context. Reason: Pallid primary neurons have a modest neurite-extension phenotype, but the inspected experiments do not independently resolve a dendrite-specific morphogenesis step. The exact donor morphology assay remains unverified. |
| GO:0048840 otolith development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Pallidin loss disrupts otolith formation in mice. Reason: The complete normal PMID:10610180 abstract explicitly identifies abnormal otolith formation among pallid mouse phenotypes. This provides positive target-relevant support for retaining the existing developmental transfer as non-core. It is not evidence for a direct human calcium-deposition enzyme or an isolated otolith-assembly reaction. Supporting Evidence: |
| GO:0050942 positive regulation of pigment cell differentiation | IDA PMID:17182842 BLOC-1 is required for cargo-specific sorting from vacuolar ... | UNDECIDED | Summary: The specific positive regulation of pigment cell differentiation assertion requires its unresolved source context. Reason: GO:0050942 concerns acquisition of a differentiated pigment-cell state. The selected human PaHA experiments restore pigment and cargo sorting in established melanocyte lines, not necessarily differentiation. The precise curator basis may include material not inspected; retain the experimental assertion as undecided. Supporting Evidence: |
| GO:0051015 actin filament binding | IDA PMID:12019270 BLOC-1, a novel complex containing the pallidin and muted pr... | KEEP AS NON CORE | Summary: Pallidin-containing material associates with filamentous actin. Reason: Selected PMID:12019270 methods and results show pallidin-containing cytosolic material sedimenting with purified F-actin and tagged human pallidin at perinuclear actin structures. The authors explicitly leave direct binding versus mediation by other actin-associated proteins unresolved. Preserve the experimental and transferred association as non-core without assigning pallidin an actin-polymerizing or crosslinking mechanism; the filamentous-actin part_of assertion is read as association, not incorporation as an actin monomer. Supporting Evidence: |
| GO:0051015 actin filament binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Pallidin-containing material associates with filamentous actin. Reason: Selected PMID:12019270 methods and results show pallidin-containing cytosolic material sedimenting with purified F-actin and tagged human pallidin at perinuclear actin structures. The authors explicitly leave direct binding versus mediation by other actin-associated proteins unresolved. Preserve the experimental and transferred association as non-core without assigning pallidin an actin-polymerizing or crosslinking mechanism; the filamentous-actin part_of assertion is read as association, not incorporation as an actin monomer. Supporting Evidence: |
| GO:0051639 actin filament network formation | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific actin filament network formation assertion requires its unresolved source context. Reason: The selected actin study establishes association with F-actin but leaves direct versus mediated binding unresolved. It does not demonstrate a pallidin-driven filament-network assembly reaction, and the mouse donor experiment remains unverified. Supporting Evidence: |
| GO:0055088 lipid homeostasis | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific lipid homeostasis assertion requires its unresolved source context. Reason: A 2005 primary Regensburg thesis reports altered lipid profiles in pooled sera from four pallidin-knockout and four control mice. This is positive target-relevant evidence, but the limited pooled comparison, proposed rather than established maintenance mechanism, and unresolved current donor-source edge leave the specific homeostasis assignment undecided. It is not evidence against a lipid role. |
| GO:0060090 molecular adaptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: Pallidin contributes to the BLOC-1 molecular assembly that coordinates trafficking proteins. Reason: GO:0060090 concerns stoichiometric association of two or more proteins to coordinate their function. The inspected human reconstitution identifies pallidin contacts with both BLOS1 and Cappuccino in a stable ternary assembly, within the functional BLOC-1 octamer. This supports an adaptor/scaffold interpretation without an autonomous motor or enzyme claim. The curated IBA is retained; donor count is not used to challenge its ancestral node. |
| GO:0060090 molecular adaptor activity | IEA GO_REF:0000107 | ACCEPT | Summary: Pallidin contributes to the BLOC-1 molecular assembly that coordinates trafficking proteins. Reason: GO:0060090 concerns stoichiometric association of two or more proteins to coordinate their function. The inspected human reconstitution identifies pallidin contacts with both BLOS1 and Cappuccino in a stable ternary assembly, within the functional BLOC-1 octamer. This supports an adaptor/scaffold interpretation without an autonomous motor or enzyme claim. The curated IBA is retained; donor count is not used to challenge its ancestral node. |
| GO:0060155 platelet dense granule organization | IEA GO_REF:0000107 | ACCEPT | Summary: Pallidin-containing BLOC-1 contributes to platelet dense-granule organization. Reason: The normal pallid-gene abstract explicitly links loss of pallidin to platelet storage-pool deficiency, and the human BLOC-1 assembly studies place it in lysosome-related-organelle biogenesis. Retain this organelle role. The retraction of the 2011 human HPS9 paper does not invalidate the independent mouse evidence or all subsequent human disease reports. |
| GO:0070328 triglyceride homeostasis | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific triglyceride homeostasis assertion requires its unresolved source context. Reason: The selected 2005 primary thesis reports reduced triglycerides in separated VLDL fractions from pooled pallidin-knockout mouse sera. The actual current donor citation and a triglyceride-maintenance mechanism remain unresolved; proposed secretion or LCAT explanations are not pallidin catalytic evidence. Preserve the source as undecided rather than deny the reported biochemical phenotype. |
| GO:0070938 contractile ring | IEA GO_REF:0000107 | UNDECIDED | Summary: Specific localization to the cytokinetic contractile ring remains unresolved. Reason: GO:0070938 describes a cytoskeletal ring on the cytoplasmic side of the membrane. Pallidin’s cytosolic and actin-associated properties are compatible with that topology, unlike an ER-lumen claim, but do not establish localization to the cytokinetic ring. The exact mouse localization experiment remains unverified, so this electronic annotation remains UNDECIDED. |
| GO:0071364 cellular response to epidermal growth factor stimulus | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific cellular response to epidermal growth factor stimulus assertion requires its unresolved source context. Reason: The exact mouse EGF-response experiment remains unverified; no receptor-signalling function is inferred solely from endosomal trafficking. |
| GO:0072657 protein localization to membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific protein localization to membrane assertion requires its unresolved source context. Reason: The precise mouse protein-to-membrane localization assay remains unverified. BLOC-1 cargo delivery is established, but this general term could cover distinct cargo and membrane contexts. |
| GO:0072659 protein localization to plasma membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific protein localization to plasma membrane assertion requires its unresolved source context. Reason: The precise mouse plasma-membrane cargo assay remains unverified. Tyrp1 accumulation at the surface of pallid melanocytes is a missorting phenotype, not evidence that pallidin directly delivers that cargo to the plasma membrane. Supporting Evidence: |
| GO:0097006 regulation of plasma lipoprotein particle levels | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific regulation of plasma lipoprotein particle levels assertion requires its unresolved source context. Reason: Selected primary mouse thesis data concern lipid content in separated plasma fractions, including altered HDL lipids and VLDL triglycerides. These composition measurements do not by themselves establish regulation of lipoprotein particle numbers. The current donor-source edge and adequate particle-level assay remain unresolved; retain UNDECIDED. |
| GO:0097487 multivesicular body, internal vesicle | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific multivesicular body, internal vesicle assertion requires its unresolved source context. Reason: BLOC-1 acts at cytoplasmic endosomal surfaces, but that does not establish pallidin within internal intraluminal vesicles. The exact donor ultrastructural or biochemical evidence remains unverified. |
| GO:0098975 postsynapse of neuromuscular junction | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The fly pallidin donor is detected on the postsynaptic side of the neuromuscular junction. Reason: Official primary evidence for PMID:28317021 includes antibody localization in postsynaptic muscle as well as presynaptic neuronal structures. This supports the source fly donor context, and the ancestral IBA is retained as non-core. It is not presented as direct localization of endogenous human pallidin or as a newly reconstructed PAINT node assignment. |
| GO:0099640 axo-dendritic protein transport | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BLOC-1 supports delivery of selected neuronal membrane cargo. Reason: Selected PMID:21998198 experiments include pallid mouse fibroblasts and dentate-gyrus cargo distribution, together with human neuronal-cell complexes containing endogenous pallidin. These support the neuronal trafficking pathway and the curator-mediated orthology inferences, rather than pallidin acting as an axonal motor or transporting every mature synaptic vesicle. Keep this neuronal specialization as non-core. |
| GO:1903441 protein localization to ciliary membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific protein localization to ciliary membrane assertion requires its unresolved source context. Reason: The exact pallidin-dependent ciliary-membrane cargo assay remains unverified. Results for other BLOC-1 subunits do not by themselves establish the target-specific step. |
| GO:1904115 axon cytoplasm | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: An axonal cytoplasmic context is consistent with neuronal cargo trafficking. Reason: This is the logical cellular-location consequence of the retained anterograde axonal-transport annotation. Selected mouse neuronal cargo experiments support the pathway, but do not independently image endogenous human pallidin throughout the axoplasm. Retain the inference as non-core. Supporting Evidence: |
| GO:1990742 microvesicle | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific microvesicle assertion requires its unresolved source context. Reason: GO:1990742 denotes extracellular microvesicles. The inspected PMID:21998198 small-vesicle preparation is made from homogenized PC12 cells and concerns intracellular vesicles. This distinction does not prove the donor is wrong, but the actual extracellular-vesicle localization evidence remains unverified. |
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Download this section (compressed HTML)Q: Which direct pallidin interfaces connect the BLOC-1 scaffold to syntaxins, AP-3 and actin-associated machinery without merely destabilizing the octamer?
Q: Which mouse-derived developmental, spatial and metabolic annotations reflect a direct pallidin activity, and which are downstream consequences of organelle dysfunction?
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