Apolipoprotein B is the persistent lipid-binding scaffold of triglyceride- and cholesterol-rich lipoproteins. Hepatic apoB100 forms the structural framework of VLDL and remains on IDL and LDL as the particles are remodelled in circulation. Intestinal RNA editing produces the shorter apoB48 product, which supports chylomicron assembly and persists in chylomicron remnants. Nascent apoB acquires lipid in the endoplasmic reticulum with assistance from microsomal triglyceride transfer protein and is exported as lipoprotein cargo. ApoB100 also presents LDL-receptor recognition surfaces that couple lipid carriage to particle clearance. ApoB48 lacks the canonical apoB100 LDLR-binding region; apoE can instead mediate remnant recognition. Intracellular quality-control pools coexist with the principal extracellular carrier role.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005319 lipid carrier activity | IEA GO_REF:0000002 | ACCEPT | Summary: Established lipid carrier activity fits the principal apoB role. Reason: The InterPro carrier mapping agrees with apoB lipid-associated amphipathic domains and the actual human LDL structural study 39662503. ApoB provides the persistent lipid-binding scaffold of circulating particles, fitting lipid carrier activity. This does not equate bulk particle carriage with the narrower aqueous cholesterol-transfer reaction. Supporting Evidence: PMID:39662503 an approximately 61-nm-long continuous amphipathic Ξ²-sheet that wraps around the LDL particle like a belt. |
| GO:0005515 protein binding | IPI PMID:16203724 Hepatitis C virus nonstructural proteins inhibit apolipoprot... | KEEP AS NON CORE | Summary: Retain protein binding in the reported contextual role. Reason: The available 16203724 abstract explicitly reports apoB binding to hepatitis C NS5A. Retain this reported virus-associated interaction without claiming a physiological cargo-adaptor mechanism or making it a principal apoB function; the precise full-paper construct/interface was not independently inspected. Supporting Evidence: PMID:16203724 Further evidence is presented for the interaction between the HCV nonstructural protein 5A and apoB100. |
| GO:0005515 protein binding | IPI PMID:21911577 A physical interaction network of dengue virus and human pro... | UNDECIDED | Summary: The source-specific protein binding assertion remains unresolved. Reason: The 21911577 dengue interactome abstract and UniProt cross-reference do not expose the apoB/NS3 pair-specific target table or tested constructs. Those source-local experiments remain unadjudicated, so preserve the positive IPI assertion as uncertain rather than rejecting it or inventing a specific activity. |
| GO:0005515 protein binding | IPI PMID:22580899 Proprotein convertase subtilisin/kexin type 9 interacts with... | KEEP AS NON CORE | Summary: Retain protein binding in the reported contextual role. Reason: The 22580899 abstract reports endogenous PCSK9βapoB association in hepatocytes in a study of three mouse models, with reduced apoB degradation and increased secretion. This supports the reported association as a contextual interaction; it does not establish an apoB enzyme or adaptor activity. Human-specific reagent details are not claimed from the mouse-focused abstract. |
| GO:0005515 protein binding | IPI PMID:24447298 LDL receptor/lipoprotein recognition: endosomal weakening of... | MODIFY | Summary: Refine the experimentally measured LDL-receptor interaction. Reason: In the actual 24447298 Results and peptide-design/SPR/NMR Methods, defined apoB site A/B peptides bind LDLR repeat LR5, with sequence/randomized controls and calcium/pH dependence. The non-engineered peptide sequences match P04114. Replace generic binding with low-density lipoprotein particle receptor binding, retaining the isolated-peptide limitation rather than claiming that this experiment measured intact-particle uptake. Proposed replacements: low-density lipoprotein particle receptor binding Supporting Evidence: PMID:24447298 We have used NMR and SPR to characterize the complexes formed by LR5 and three peptides encompassing the putative binding regions of ApoB (site A and site B) and ApoE. |
| GO:0005515 protein binding | IPI PMID:25108285 Novel missense MTTP gene mutations causing abetalipoproteine... | KEEP AS NON CORE | Summary: Retain protein binding in the reported contextual role. Reason: The complete 25108285 abstract reports binding of each tested MTP missense variant to apoB17 and apoB48, despite differences in MTP lipid transfer and particle secretion. Retain the specific positive apoBβMTP association without assigning MTP lipid-transfer chemistry to apoB or asserting a purified binary interface. Supporting Evidence: PMID:25108285 all missense MTTP mutations interacted with apoB17, apoB48, and protein disulfide isomerase. |
| GO:0005515 protein binding | IPI PMID:26224785 Novel Abetalipoproteinemia Missense Mutation Highlights the ... | KEEP AS NON CORE | Summary: Retain protein binding in the reported contextual role. Reason: Actual 26224785 targeted Results/Methods report apoB17βMTP co-immunoprecipitation and distinguish retained apoB association from the D169V defect in PDI association/lipid transfer. Human apoB48 is explicitly identified in secretion constructs; apoB17 reagent species is not assumed from that. The positive interaction remains valid but is not itself a more specific apoB molecular mechanism. Supporting Evidence: PMID:26224785 Although D169V was expressed in the endoplasmic reticulum and interacted with apolipoprotein B (apoB) 17, it was unable to bind protein disulfide isomerase, transfer lipids, and support apoB secretion. |
| GO:0005515 protein binding | IPI PMID:27138255 TANGO1 and Mia2/cTAGE5 (TALI) cooperate to export bulky pre-... | KEEP AS NON CORE | Summary: Retain protein binding in the reported contextual role. Reason: Actual 27138255 Results and co-immunoprecipitation Methods show endogenous apoB association with TANGO1 in human secretory cells during ER export. The authors leave a direct interface versus an intervening component unresolved. ApoB is the recruited lipoprotein cargo, so these data support association without giving apoB the receptor/adaptor function. Preserve the original partner identifier. Supporting Evidence: PMID:27138255 TANGO1 binds TALI, and both interact with apolipoprotein B (ApoB) and are necessary for the recruitment of ApoB-containing lipid particles to ER exit sites for their subsequent export. |
| GO:0005515 protein binding | IPI PMID:27138255 TANGO1 and Mia2/cTAGE5 (TALI) cooperate to export bulky pre-... | KEEP AS NON CORE | Summary: Retain protein binding in the reported contextual role. Reason: Actual 27138255 Results and co-immunoprecipitation Methods show endogenous apoB association with TALI in human secretory cells during ER export. The authors leave a direct interface versus an intervening component unresolved. ApoB is the recruited lipoprotein cargo, so these data support association without giving apoB the receptor/adaptor function. Preserve the original partner identifier. Supporting Evidence: PMID:27138255 TANGO1 binds TALI, and both interact with apolipoprotein B (ApoB) and are necessary for the recruitment of ApoB-containing lipid particles to ER exit sites for their subsequent export. |
| GO:0005515 protein binding | IPI PMID:27487388 Structure-function analyses of microsomal triglyceride trans... | UNDECIDED | Summary: The source-specific protein binding assertion remains unresolved. Reason: The 27487388 abstract describes the MTP D361Y defect in PDI association, lipid transfer and lipoprotein secretion but does not expose the apoB-specific interaction assay. The relevant full experiment remains unread; preserve this IPI pair as uncertain rather than replacing it using a different MTP paper. |
| GO:0005515 protein binding | IPI PMID:8245722 Identification of disulfide-linked apolipoprotein species in... | KEEP AS NON CORE | Summary: Retain protein binding in the reported contextual role. Reason: The actual 8245722 abstract identifies disulfide-linked apoB100βapoAII species in human VLDL/LDL, enriched in hyperlipidemic subjects. This is positive association evidence and is retained as a contextual interaction, without an unsupported specific carrier-adaptor or enzyme-binding refinement. Supporting Evidence: PMID:8245722 the demonstration of the existence of the disulfide-linked species apolipoprotein B-100:A-II and B-100:C-IIToronto in the very low density and low density lipoproteins |
| GO:0005543 phospholipid binding | IDA PMID:7126555 Sulfhydryl chemistry and solubility properties of human plas... | UNDECIDED | Summary: The source-specific phospholipid binding assertion remains unresolved. Reason: The normal 7126555 record has bibliographic metadata without an abstract or accessible target assay. ApoB binds particle lipids generally, but the source-specific phospholipid experiment has not been verified. Preserve the experimental assertion as unresolved rather than inferring its detailed specificity from the structural paper. |
| GO:0005576 extracellular region | EXP PMID:22580899 Proprotein convertase subtilisin/kexin type 9 interacts with... | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: Secretion of apoB-containing particles is reported in the 22580899 study and is independently established by human plasma particle assays and native human LDL structures. Accept extracellular apoB as a principal location while retaining the study's mouse-model boundary; no human-specific PCSK9 assay is inferred. Supporting Evidence: PMID:4363408 The assay measures not only the ApoB content of beta-lipoproteins (low density lipoproteins [LDL]) but also that contained in the other lipoproteins in plasma. |
| GO:0005576 extracellular region | EXP PMID:26224785 Novel Abetalipoproteinemia Missense Mutation Highlights the ... | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: Actual 26224785 Methods include human apoB48 secretion constructs, and the study measures secreted apoB-containing particles. Extracellular apoB is a principal location of its carrier role; this does not make apoB the lipid-transfer enzyme. Supporting Evidence: PMID:26224785 cells expressing D169V had significantly lower amounts of secreted apoB48 compared to cells expressing MTP (Fig 1B). |
| GO:0005576 extracellular region | HDA PMID:27068509 Extracellular matrix remodelling in response to venous hyper... | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The HDA source 27068509 is a secreted/plasma-protein dataset; its exact target table was not reanalyzed. Extracellular apoB is independently directly established by human plasma lipoprotein measurements and 39662503 native human LDL, so accept this clearly correct location while deferring to the curated dataset for the individual detection. Supporting Evidence: PMID:4363408 The assay measures not only the ApoB content of beta-lipoproteins (low density lipoproteins [LDL]) but also that contained in the other lipoproteins in plasma. |
| GO:0005576 extracellular region | IEA GO_REF:0000044 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The UniProt secreted-location mapping is independently corroborated by human plasma apoB measurements and human LDL structural work. Extracellular particles are a principal setting of apoB lipid carriage and receptor recognition. Supporting Evidence: PMID:4363408 The assay measures not only the ApoB content of beta-lipoproteins (low density lipoproteins [LDL]) but also that contained in the other lipoproteins in plasma. |
| GO:0005576 extracellular region | ISS PMID:22261194 Proteomics analysis of cardiac extracellular matrix remodeli... | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The original ISS donor is porcine Q29021 and 22261194 is a porcine reference-proteome study with limited human validation. Retain the source boundary; secretion is independently established for human apoB, so the broad extracellular location is sound without reconstructing a human experiment in that paper. Supporting Evidence: PMID:4363408 The assay measures not only the ApoB content of beta-lipoproteins (low density lipoproteins [LDL]) but also that contained in the other lipoproteins in plasma. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-171122 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-171122 summary places apoB-containing lipoprotein in an extracellular context: LDL binds the human LDL receptor through apoB100 at the cell surface. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-171122 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-174587 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-174587 summary places apoB-containing lipoprotein in an extracellular context: apoB48-containing chylomicrons are exported from the ER to the extracellular space. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-174587 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-174657 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-174657 summary places apoB-containing lipoprotein in an extracellular context: apoB48-containing remnants bind LDLR through apoE, not an apoB48 LDLR site. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-174657 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-174660 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-174660 summary places apoB-containing lipoprotein in an extracellular context: nascent chylomicrons exchange apolipoproteins during extracellular maturation. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-174660 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-174690 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-174690 summary places apoB-containing lipoprotein in an extracellular context: triglyceride-depleted chylomicrons donate apoA/apoC proteins to HDL. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-174690 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-174739 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-174739 summary places apoB-containing lipoprotein in an extracellular context: apoE-rich remnants associate in the extracellular space of Disse. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-174739 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-174757 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-174757 summary places apoB-containing lipoprotein in an extracellular context: LPL hydrolyzes triglyceride on extracellular chylomicrons with apoCII as its cofactor. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-174757 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-176879 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-176879 summary places apoB-containing lipoprotein in an extracellular context: lipoprotein(a) forms through apo(a) association with the apoB-containing LDL particle. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-176879 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-203130 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-203130 summary places apoB-containing lipoprotein in an extracellular context: oxidized LDL engages OLR1 outside the cell. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-203130 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2187261 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2187261 summary places apoB-containing lipoprotein in an extracellular context: COLEC12 recognizes extracellular lipoprotein ligands. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2187261 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2187332 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2187332 summary places apoB-containing lipoprotein in an extracellular context: intestinal chylomicrons enter the circulation for delivery to the liver. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2187332 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2197646 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2197646 summary places apoB-containing lipoprotein in an extracellular context: SR-BI engages extracellular lipoprotein particles. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2197646 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2197770 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2197770 summary places apoB-containing lipoprotein in an extracellular context: STAB1 recognizes modified extracellular LDL. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2197770 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2203479 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2203479 summary places apoB-containing lipoprotein in an extracellular context: STAB2 recognizes modified extracellular lipoprotein particles. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2203479 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2247511 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2247511 summary places apoB-containing lipoprotein in an extracellular context: STAB2 internalizes ligand-bearing complexes from the cell surface. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2247511 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2247512 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2247512 summary places apoB-containing lipoprotein in an extracellular context: CD36 binds extracellular oxidized LDL before internalization. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2247512 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2247513 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2247513 summary places apoB-containing lipoprotein in an extracellular context: STAB1 internalizes extracellular modified LDL. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2247513 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2247514 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2247514 summary places apoB-containing lipoprotein in an extracellular context: SCARF1 recognizes extracellular modified LDL. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2247514 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2395768 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2395768 summary places apoB-containing lipoprotein in an extracellular context: LPL acts on triglyceride carried in extracellular chylomicrons. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2395768 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2395784 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2395784 summary places apoB-containing lipoprotein in an extracellular context: chylomicrons mature by acquiring and exchanging surface apolipoproteins. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2395784 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2404131 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2404131 summary places apoB-containing lipoprotein in an extracellular context: apoE-bearing chylomicron remnants undergo extracellular HSPG/LRP engagement before uptake. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2404131 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2423785 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2423785 summary places apoB-containing lipoprotein in an extracellular context: chylomicron remnants associate with hepatocyte-surface heparan sulfate proteoglycans through apoE. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2423785 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2507854 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2507854 summary places apoB-containing lipoprotein in an extracellular context: MSR1 binds extracellular modified LDL before uptake. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2507854 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2512800 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-2512800 summary places apoB-containing lipoprotein in an extracellular context: SR-BI selectively transfers lipids from bound extracellular particles. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-2512800 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-266350 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-266350 summary places apoB-containing lipoprotein in an extracellular context: CETP exchanges neutral lipids between extracellular lipoproteins. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-266350 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2981040 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The R-HSA-2981040 summary primarily describes microbial COLEC12 uptake and infers other ligands, so it is not an independent apoB localization assay. The broad extracellular location is nevertheless directly established for human apoB by plasma/LDL studies and is accepted on that independent evidence, without endorsing a particular COLEC12 uptake mechanism. Supporting Evidence: Reactome:R-HSA-2981040 PMID:4363408 The assay measures not only the ApoB content of beta-lipoproteins (low density lipoproteins [LDL]) but also that contained in the other lipoproteins in plasma. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-432121 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-432121 summary places apoB-containing lipoprotein in an extracellular context: LDL engages platelet LRP8. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-432121 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-432129 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-432129 summary places apoB-containing lipoprotein in an extracellular context: FGR phosphorylates a receptor complex assembled after extracellular LDL engagement. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-432129 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-8854408 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-8854408 summary places apoB-containing lipoprotein in an extracellular context: APOBR binds apoB48-containing triglyceride-rich lipoproteins and selected hypertriglyceridemic apoB100 VLDL. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-8854408 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-8854462 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-8854462 summary places apoB-containing lipoprotein in an extracellular context: VLDLR binds circulating triglyceride-rich lipoproteins. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-8854462 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-8866321 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-8866321 summary places apoB-containing lipoprotein in an extracellular context: VLDL acquires apoC proteins in the circulation. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-8866321 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-8866327 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-8866327 summary places apoB-containing lipoprotein in an extracellular context: apoB100-containing VLDL is secreted from the smooth ER pathway. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-8866327 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-8869667 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-8869667 summary places apoB-containing lipoprotein in an extracellular context: oxidized LDL participates in CD36/TLR4/TLR6 receptor signaling. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-8869667 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-8948034 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-8948034 summary places apoB-containing lipoprotein in an extracellular context: extracellular LDL engagement accompanies FGR association with LRP8. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-8948034 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9707586 | ACCEPT | Summary: Established extracellular region fits the principal apoB role. Reason: The read Reactome:R-HSA-9707586 summary places apoB-containing lipoprotein in an extracellular context: extracellular heme can oxidize LDL and HDL. Extracellular apoB is also directly established by human particle studies. Accept the location; membership in this event does not assign the receptor, lipase, kinase or lipid-transfer activity to apoB. Supporting Evidence: Reactome:R-HSA-9707586 |
| GO:0005737 cytoplasm | IDA PMID:22580899 Proprotein convertase subtilisin/kexin type 9 interacts with... | KEEP AS NON CORE | Summary: Retain cytoplasm in the reported contextual role. Reason: UniProt explicitly attributes a cytoplasmic apoB pool to 22580899, whose abstract reports intracellular PCSK9βapoB association. Retain the curated intracellular pool as non-core alongside the independently observed HPA cytosolic signal, while not claiming that the mouse-focused abstract resolves a human subcellular assay or that all apoB is soluble in cytosol. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Retain cytoplasm in the reported contextual role. Reason: The UniProt cytoplasm mapping is consistent with intracellular biosynthetic/quality-control apoB pools and HPA cytosolic staining. Retain this broad location as non-core relative to extracellular lipid carriage; it does not supersede secretory-pathway luminal localization. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005769 early endosome | TAS Reactome:R-HSA-2404131 | KEEP AS NON CORE | Summary: Retain early endosome in the reported contextual role. Reason: The R-HSA-2404131 pathway places internalized apoE-bearing remnant cargo in the endosomal route after hepatic uptake. Retain early-endosomal presence as a contextual cargo location; apoB is not inferred to perform LRP/HSPG uptake or retinyl-ester hydrolysis. Supporting Evidence: Reactome:R-HSA-2404131 |
| GO:0005769 early endosome | TAS Reactome:R-HSA-2404140 | UNDECIDED | Summary: The source-specific early endosome assertion remains unresolved. Reason: The read Reactome:R-HSA-2404140 summary locates retinyl-ester hydrolase activity in endosomal preparations, largely from rodents, but does not resolve the apoB polypeptide or an apoB-specific early-endosome experiment. The exact source-to-entity localization remains uncertain, not disproven by this limited summary. |
| GO:0005769 early endosome | TAS Reactome:R-HSA-2429643 | UNDECIDED | Summary: The source-specific early endosome assertion remains unresolved. Reason: The read Reactome:R-HSA-2429643 summary locates retinyl-ester hydrolase activity in endosomal preparations, largely from rodents, but does not resolve the apoB polypeptide or an apoB-specific early-endosome experiment. The exact source-to-entity localization remains uncertain, not disproven by this limited summary. |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000107 | ACCEPT | Summary: Established endoplasmic reticulum fits the principal apoB role. Reason: The original electronic transfer names mouse E9Q414/ENSMUSP00000036044. Human apoB synthesis/lipidation and direct human secretory-cell ER-export work independently support an ER location, so accept the broad compartment without claiming the donor annotation chain was reconstructed. Supporting Evidence: PMID:27138255 TANGO1 binds TALI, and both interact with apolipoprotein B (ApoB) and are necessary for the recruitment of ApoB-containing lipid particles to ER exit sites for their subsequent export. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-174587 | ACCEPT | Summary: Established endoplasmic reticulum lumen fits the principal apoB role. Reason: R-HSA-174587 describes assembly/export of apoB48-containing chylomicrons from the ER lumen. This luminal site is part of apoB particle biogenesis and agrees with human apoB export work, so accept the location as core. Supporting Evidence: Reactome:R-HSA-174587 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-174731 | UNDECIDED | Summary: The source-specific endoplasmic reticulum lumen assertion remains unresolved. Reason: R-HSA-174731 explicitly leaves the degradation site of unlipidated apoB48 unresolved between ER and cytosolic proteasomes. General ER biosynthesis does not resolve this event-specific ER-lumen assertion. Retain uncertainty for the precise degradation pool rather than treating the alternatives as a refutation of ER localization overall. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-174741 | ACCEPT | Summary: Established endoplasmic reticulum lumen fits the principal apoB role. Reason: R-HSA-174741 describes nascent apoB48 binding lipid in the ER lumen with MTP assistance. ApoB supplies the lipid-binding scaffold while MTP performs transfer. Accept the luminal assembly location without assigning MTP chemistry to apoB. Supporting Evidence: Reactome:R-HSA-174741 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-8952289 | UNDECIDED | Summary: The source-specific endoplasmic reticulum lumen assertion remains unresolved. Reason: R-HSA-8952289 describes FAM20C phosphorylation of secreted substrates but its available summary does not expose the apoB-specific substrate entry or ER-lumen evidence. The precise annotation remains unresolved even though apoB biosynthesis involves the ER. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-174786 | KEEP AS NON CORE | Summary: Retain endoplasmic reticulum membrane in the reported contextual role. Reason: R-HSA-174786 places nascent apoB48 lipidation at the ER membrane. Retain this biosynthetic membrane-associated state as non-core localization, distinct from an integral membrane role; MTP carries out lipid transfer. Supporting Evidence: Reactome:R-HSA-174786 |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-8866308 | KEEP AS NON CORE | Summary: Retain endoplasmic reticulum membrane in the reported contextual role. Reason: R-HSA-8866308 describes pre-VLDL moving from rough-ER membrane association to the smooth-ER lumen. Retain the explicitly modeled precursor membrane-associated state as non-core, not a permanent transmembrane apoB topology. Supporting Evidence: Reactome:R-HSA-8866308 |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-8866329 | KEEP AS NON CORE | Summary: Retain endoplasmic reticulum membrane in the reported contextual role. Reason: R-HSA-8866329 describes MTP lipidation of newly synthesized apoB100 in the rough ER, initially associated with its membrane. Retain transient membrane association as non-core; apoB is the structural lipid recipient and MTP is the transfer factor. Supporting Evidence: Reactome:R-HSA-8866329 |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-8952289 | UNDECIDED | Summary: The source-specific endoplasmic reticulum membrane assertion remains unresolved. Reason: The generic FAM20C substrate summary R-HSA-8952289 does not resolve an apoB-specific ER-membrane entity or its topology. Preserve the assertion as uncertain pending the underlying substrate/compartment evidence, without arguing that a secreted protein cannot contact ER membranes. |
| GO:0005790 smooth endoplasmic reticulum | TAS Reactome:R-HSA-8866304 | ACCEPT | Summary: Established smooth endoplasmic reticulum fits the principal apoB role. Reason: R-HSA-8866304 describes further lipid incorporation into apoB100-containing VLDL in the smooth ER. This is a particle-assembly location, with apoB providing the structural lipid scaffold. Supporting Evidence: Reactome:R-HSA-8866304 |
| GO:0005790 smooth endoplasmic reticulum | TAS Reactome:R-HSA-8866308 | ACCEPT | Summary: Established smooth endoplasmic reticulum fits the principal apoB role. Reason: R-HSA-8866308 explicitly moves pre-VLDL to the smooth-ER lumen during maturation. Accept smooth ER as an assembly compartment, distinct from the preceding membrane-associated precursor state. Supporting Evidence: Reactome:R-HSA-8866308 |
| GO:0005790 smooth endoplasmic reticulum | TAS Reactome:R-HSA-8866327 | ACCEPT | Summary: Established smooth endoplasmic reticulum fits the principal apoB role. Reason: R-HSA-8866327 describes export of mature apoB100-containing VLDL from the smooth-ER pathway to the extracellular space. Accept the assembly/secretion compartment without assigning export-machinery activity to apoB. Supporting Evidence: Reactome:R-HSA-8866327 |
| GO:0005811 lipid droplet | EXP PMID:28183703 AUP1 (Ancient Ubiquitous Protein 1) Is a Key Determinant of ... | KEEP AS NON CORE | Summary: Retain lipid droplet in the reported contextual role. Reason: The actual 28183703 original Fig5 Results/Discussion place a fraction of HepG2 apoB with AUP1 at lipid-droplet surfaces, enhanced by lipid loading/proteasome inhibition and discussed in quality control. Retain this experimental contextual pool without making it the principal site of circulating apoB activity. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005811 lipid droplet | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Retain lipid droplet in the reported contextual role. Reason: The lipid-droplet UniProt mapping has direct contextual support from 28183703 human HepG2 imaging. Preserve it as non-core quality-control localization, not as evidence that all apoB occupies lipid droplets. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005829 cytosol | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Retain cytosol in the reported contextual role. Reason: The actual HPA APOB table reports supported cytosol staining in Hep-G2 with HPA049793, alongside vesicles. This is positive evidence for an intracellular pool and is retained as non-core; no reanalysis of images or antibody specificity is claimed. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2187332 | UNDECIDED | Summary: The precise source-specific assertion remains unresolved. Reason: The actual Reactome component chain explicitly maps this nascent chylomicron to APOB(28-2179), UniProt:P04114, via R-HSA-2395787, R-HSA-2395777 and R-HSA-2395786, all labeled cytosol. Thus the apoB48 identity is resolved. What remains uncertain is the physical topology represented by the cytosolic nascent-particle label during retinyl-ester loading/secretion, relative to the independently established ER/secretory-lumen pool. The HPA cytosolic observation is retained separately and neither proves this particular particle topology nor permits a categorical assertion that APOB is never cytosolic. Retain the source-specific uncertainty, not a missing-gene claim. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2395764 | UNDECIDED | Summary: The precise source-specific assertion remains unresolved. Reason: The actual Reactome component chain explicitly maps this nascent chylomicron to APOB(28-2179), UniProt:P04114, via R-HSA-2395787, R-HSA-2395777 and R-HSA-2395786, all labeled cytosol. Thus the apoB48 identity is resolved. What remains uncertain is the physical topology represented by the cytosolic nascent-particle label during retinyl-ester loading/secretion, relative to the independently established ER/secretory-lumen pool. The HPA cytosolic observation is retained separately and neither proves this particular particle topology nor permits a categorical assertion that APOB is never cytosolic. Retain the source-specific uncertainty, not a missing-gene claim. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-171122 | KEEP AS NON CORE | Summary: Retain plasma membrane in the reported contextual role. Reason: The read Reactome:R-HSA-171122 summary states that apoB100-containing LDL binds LDLR at the cell surface. Retain this surface-associated cargo/receptor-complex location as non-core; it is not an integral plasma-membrane or cytosolic coat-component role for apoB. Supporting Evidence: Reactome:R-HSA-171122 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-171141 | KEEP AS NON CORE | Summary: Retain plasma membrane in the reported contextual role. Reason: The read Reactome:R-HSA-171141 summary states that receptor-bound LDL is gathered into clathrin-coated pits. Retain this surface-associated cargo/receptor-complex location as non-core; it is not an integral plasma-membrane or cytosolic coat-component role for apoB. Supporting Evidence: Reactome:R-HSA-171141 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-174657 | KEEP AS NON CORE | Summary: Retain plasma membrane in the reported contextual role. Reason: The read Reactome:R-HSA-174657 summary states that apoE-bearing apoB48 remnants bind cell-surface LDLR. Retain this surface-associated cargo/receptor-complex location as non-core; it is not an integral plasma-membrane or cytosolic coat-component role for apoB. Supporting Evidence: Reactome:R-HSA-174657 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-174706 | KEEP AS NON CORE | Summary: Retain plasma membrane in the reported contextual role. Reason: The read Reactome:R-HSA-174706 summary states that receptor-bound remnants enter coated pits. Retain this surface-associated cargo/receptor-complex location as non-core; it is not an integral plasma-membrane or cytosolic coat-component role for apoB. Supporting Evidence: Reactome:R-HSA-174706 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8863471 | KEEP AS NON CORE | Summary: Retain the source-defined receptor-associated particle pool as non-core. Reason: The actual Reactome component hierarchy for R-HSA-8863471 retains LDL bound to LDLR through DAB2/LDLRAP1 within the plasma-membrane CLASP cargo set. LDL entity R-HSA-171112 explicitly contains APOB(28-4563). This supplies positive contextual localization during DAB2/LDLRAP1 binding to the LDL receptor, independently of whether the reaction summary names APOB. Retain this transient receptor-associated cargo pool as non-core. The GO plasma-membrane definition includes associated proteins; this does not imply that APOB spans the bilayer or performs the coat, kinase, phosphatase or GTPase activity. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867754 | KEEP AS NON CORE | Summary: Retain the source-defined receptor-associated particle pool as non-core. Reason: The actual Reactome component hierarchy for R-HSA-8867754 retains LDL bound to LDLR through DAB2/LDLRAP1 within the plasma-membrane CLASP cargo set. LDL entity R-HSA-171112 explicitly contains APOB(28-4563). This supplies positive contextual localization during BAR-domain protein recruitment to the coated pit, independently of whether the reaction summary names APOB. Retain this transient receptor-associated cargo pool as non-core. The GO plasma-membrane definition includes associated proteins; this does not imply that APOB spans the bilayer or performs the coat, kinase, phosphatase or GTPase activity. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867756 | KEEP AS NON CORE | Summary: Retain the source-defined receptor-associated particle pool as non-core. Reason: The actual Reactome component hierarchy for R-HSA-8867756 retains LDL bound to LDLR through DAB2/LDLRAP1 within the plasma-membrane CLASP cargo set. LDL entity R-HSA-171112 explicitly contains APOB(28-4563). This supplies positive contextual localization during CLASP and cargo incorporation into the nascent pit, independently of whether the reaction summary names APOB. Retain this transient receptor-associated cargo pool as non-core. The GO plasma-membrane definition includes associated proteins; this does not imply that APOB spans the bilayer or performs the coat, kinase, phosphatase or GTPase activity. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868071 | KEEP AS NON CORE | Summary: Retain the source-defined receptor-associated particle pool as non-core. Reason: The actual Reactome component hierarchy for R-HSA-8868071 retains LDL bound to LDLR through DAB2/LDLRAP1 within the plasma-membrane CLASP cargo set. LDL entity R-HSA-171112 explicitly contains APOB(28-4563). This supplies positive contextual localization during clathrin-dependent recruitment of PIK3C2A, independently of whether the reaction summary names APOB. Retain this transient receptor-associated cargo pool as non-core. The GO plasma-membrane definition includes associated proteins; this does not imply that APOB spans the bilayer or performs the coat, kinase, phosphatase or GTPase activity. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868072 | KEEP AS NON CORE | Summary: Retain the source-defined receptor-associated particle pool as non-core. Reason: The actual Reactome component hierarchy for R-HSA-8868072 retains LDL bound to LDLR through DAB2/LDLRAP1 within the plasma-membrane CLASP cargo set. LDL entity R-HSA-171112 explicitly contains APOB(28-4563). This supplies positive contextual localization during PIK3C2A-dependent phosphoinositide phosphorylation, independently of whether the reaction summary names APOB. Retain this transient receptor-associated cargo pool as non-core. The GO plasma-membrane definition includes associated proteins; this does not imply that APOB spans the bilayer or performs the coat, kinase, phosphatase or GTPase activity. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868230 | KEEP AS NON CORE | Summary: Retain the source-defined receptor-associated particle pool as non-core. Reason: The actual Reactome component hierarchy for R-HSA-8868230 retains LDL bound to LDLR through DAB2/LDLRAP1 within the plasma-membrane CLASP cargo set. LDL entity R-HSA-171112 explicitly contains APOB(28-4563). This supplies positive contextual localization during SNX9-dependent recruitment of actin-polymerizing factors, independently of whether the reaction summary names APOB. Retain this transient receptor-associated cargo pool as non-core. The GO plasma-membrane definition includes associated proteins; this does not imply that APOB spans the bilayer or performs the coat, kinase, phosphatase or GTPase activity. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868236 | KEEP AS NON CORE | Summary: Retain the source-defined receptor-associated particle pool as non-core. Reason: The actual Reactome component hierarchy for R-HSA-8868236 retains LDL bound to LDLR through DAB2/LDLRAP1 within the plasma-membrane CLASP cargo set. LDL entity R-HSA-171112 explicitly contains APOB(28-4563). This supplies positive contextual localization during dynamin recruitment by BAR-domain proteins, independently of whether the reaction summary names APOB. Retain this transient receptor-associated cargo pool as non-core. The GO plasma-membrane definition includes associated proteins; this does not imply that APOB spans the bilayer or performs the coat, kinase, phosphatase or GTPase activity. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868648 | KEEP AS NON CORE | Summary: Retain the source-defined receptor-associated particle pool as non-core. Reason: The actual Reactome component hierarchy for R-HSA-8868648 retains LDL bound to LDLR through DAB2/LDLRAP1 within the plasma-membrane CLASP cargo set. LDL entity R-HSA-171112 explicitly contains APOB(28-4563). This supplies positive contextual localization during SYNJ/OCRL-dependent phosphoinositide hydrolysis, independently of whether the reaction summary names APOB. Retain this transient receptor-associated cargo pool as non-core. The GO plasma-membrane definition includes associated proteins; this does not imply that APOB spans the bilayer or performs the coat, kinase, phosphatase or GTPase activity. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868651 | KEEP AS NON CORE | Summary: Retain the source-defined receptor-associated particle pool as non-core. Reason: The actual Reactome component hierarchy for R-HSA-8868651 retains LDL bound to LDLR through DAB2/LDLRAP1 within the plasma-membrane CLASP cargo set. LDL entity R-HSA-171112 explicitly contains APOB(28-4563). This supplies positive contextual localization during synaptojanin recruitment by endophilins, independently of whether the reaction summary names APOB. Retain this transient receptor-associated cargo pool as non-core. The GO plasma-membrane definition includes associated proteins; this does not imply that APOB spans the bilayer or performs the coat, kinase, phosphatase or GTPase activity. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868658 | UNDECIDED | Summary: The precise source-specific assertion remains unresolved. Reason: The actual participant hierarchy was inspected: HSPA8-driven clathrin uncoating in R-HSA-8868658 carries the LDL cargo in a clathrin-coated endocytic vesicle membrane complex, yet the nested LDL:LDLR entity R-HSA-171100 and LDL entity R-HSA-171112 retain plasma-membrane labels. APOB membership is explicit, so the uncertainty is no longer an unread cargo identity. The unresolved issue is whether this nested label is intended to assert the plasma membrane for this post-scission event or is inherited across the compartment transition. Retain UNDECIDED for that precise source-local assignment; do not infer that APOB catalyzes uncoating, or that receptor-associated APOB can never be at the cell surface. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868659 | UNDECIDED | Summary: The precise source-specific assertion remains unresolved. Reason: The actual participant hierarchy was inspected: auxilin recruitment after fission in R-HSA-8868659 carries the LDL cargo in a clathrin-coated endocytic vesicle membrane complex, yet the nested LDL:LDLR entity R-HSA-171100 and LDL entity R-HSA-171112 retain plasma-membrane labels. APOB membership is explicit, so the uncertainty is no longer an unread cargo identity. The unresolved issue is whether this nested label is intended to assert the plasma membrane for this post-scission event or is inherited across the compartment transition. Retain UNDECIDED for that precise source-local assignment; do not infer that APOB catalyzes uncoating, or that receptor-associated APOB can never be at the cell surface. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868660 | UNDECIDED | Summary: The precise source-specific assertion remains unresolved. Reason: The actual participant hierarchy was inspected: HSPA8 recruitment to the coated vesicle in R-HSA-8868660 carries the LDL cargo in a clathrin-coated endocytic vesicle membrane complex, yet the nested LDL:LDLR entity R-HSA-171100 and LDL entity R-HSA-171112 retain plasma-membrane labels. APOB membership is explicit, so the uncertainty is no longer an unread cargo identity. The unresolved issue is whether this nested label is intended to assert the plasma membrane for this post-scission event or is inherited across the compartment transition. Retain UNDECIDED for that precise source-local assignment; do not infer that APOB catalyzes uncoating, or that receptor-associated APOB can never be at the cell surface. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868661 | KEEP AS NON CORE | Summary: Retain the source-defined receptor-associated particle pool as non-core. Reason: The actual Reactome component hierarchy for R-HSA-8868661 retains LDL bound to LDLR through DAB2/LDLRAP1 within the plasma-membrane CLASP cargo set. LDL entity R-HSA-171112 explicitly contains APOB(28-4563). This supplies positive contextual localization during the plasma-membrane input immediately before dynamin-mediated scission, independently of whether the reaction summary names APOB. Retain this transient receptor-associated cargo pool as non-core. The GO plasma-membrane definition includes associated proteins; this does not imply that APOB spans the bilayer or performs the coat, kinase, phosphatase or GTPase activity. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8869438 | UNDECIDED | Summary: The precise source-specific assertion remains unresolved. Reason: The actual participant hierarchy was inspected: coat-protein dissociation in R-HSA-8869438 carries the LDL cargo in a clathrin-coated endocytic vesicle membrane complex, yet the nested LDL:LDLR entity R-HSA-171100 and LDL entity R-HSA-171112 retain plasma-membrane labels. APOB membership is explicit, so the uncertainty is no longer an unread cargo identity. The unresolved issue is whether this nested label is intended to assert the plasma membrane for this post-scission event or is inherited across the compartment transition. Retain UNDECIDED for that precise source-local assignment; do not infer that APOB catalyzes uncoating, or that receptor-associated APOB can never be at the cell surface. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8871193 | UNDECIDED | Summary: The precise source-specific assertion remains unresolved. Reason: The actual participant hierarchy was inspected: AAK1 displacement and AP-2 dephosphorylation in R-HSA-8871193 carries the LDL cargo in a clathrin-coated endocytic vesicle membrane complex, yet the nested LDL:LDLR entity R-HSA-171100 and LDL entity R-HSA-171112 retain plasma-membrane labels. APOB membership is explicit, so the uncertainty is no longer an unread cargo identity. The unresolved issue is whether this nested label is intended to assert the plasma membrane for this post-scission event or is inherited across the compartment transition. Retain UNDECIDED for that precise source-local assignment; do not infer that APOB catalyzes uncoating, or that receptor-associated APOB can never be at the cell surface. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8871194 | UNDECIDED | Summary: The precise source-specific assertion remains unresolved. Reason: The actual participant hierarchy was inspected: RAB5/GAPVD1 recruitment to AP-2 in R-HSA-8871194 carries the LDL cargo in a clathrin-coated endocytic vesicle membrane complex, yet the nested LDL:LDLR entity R-HSA-171100 and LDL entity R-HSA-171112 retain plasma-membrane labels. APOB membership is explicit, so the uncertainty is no longer an unread cargo identity. The unresolved issue is whether this nested label is intended to assert the plasma membrane for this post-scission event or is inherited across the compartment transition. Retain UNDECIDED for that precise source-local assignment; do not infer that APOB catalyzes uncoating, or that receptor-associated APOB can never be at the cell surface. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0006629 lipid metabolic process | IEA GO_REF:0000117 | ACCEPT | Summary: Retain the established broad scope with explicit source limits. Reason: Retain this broad existing metabolic annotation in agreement with the independently curated cholesterol-metabolic-process assertion from PMID:2563166, whose human apoB defect links impaired LDL-receptor recognition to altered cholesterol handling. ApoB supplies the particle scaffold and receptor-recognition surface within this pathway; the annotation does not assign lipid synthesis or hydrolysis to apoB. Lipid transport and noncovalent particle assembly are not synonyms or automatic subclasses of lipid metabolism. The exact ARBA00028591 rule was not retrievable, so its mapping is not independently reconstructed here; this is qualified retention of the established biological scope, not a claim that the electronic rule was verified. Supporting Evidence: file:human/APOB/APOB-notes.md |
| GO:0006642 triglyceride mobilization | IBA GO_REF:0000033 | UNDECIDED | Summary: The source-specific triglyceride mobilization assertion remains unresolved. Reason: The official triglyceride-mobilization term concerns release of stored triglyceride for metabolism. ApoB particle assembly/export is relevant, but the actual PTN002673834 ancestral assertion and mouse experiment have not been inspected after the bounded PAINT access failure. Leave this particular process transfer unresolved; a short donor list is not an objection and no triglyceride-hydrolase activity is implied. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN002673834 UNRESOLVED The GOA node identifier was inspected, but its IBD assertion, tree placement and MSA were not recovered in the bounded configured PAINT attempt. No donor-count or self-evidence objection is asserted. |
| GO:0006869 lipid transport | IEA GO_REF:0000002 | ACCEPT | Summary: Established lipid transport fits the principal apoB role. Reason: The InterPro lipid-transport mapping fits apoB's direct lipid-binding scaffold and circulation in chylomicrons/VLDL/LDL. ApoB physically carries lipid as part of these particles, rather than merely being a substrate of a lipid enzyme. |
| GO:0007165 signal transduction | IEA GO_REF:0000108 | UNDECIDED | Summary: The source-specific signal transduction assertion remains unresolved. Reason: This electronic signal-transduction assertion derives from receptor-ligand activity. The production TREM2 GO-CAM does model apoB as an activating ligand, but the APOB-specific 27477018 assay and its source-local scope remain unread. Keep the broad inferred process unresolved rather than assigning intracellular signal-transduction machinery to apoB. |
| GO:0008201 heparin binding | IDA PMID:16233946 The effect of heparin on structural and functional propertie... | KEEP AS NON CORE | Summary: Retain heparin binding in the reported contextual role. Reason: The 16233946 complete abstract directly measures heparin binding to human LDL and changes in apoB/heparin dynamics, with reduced LDLR binding. Retain this surface-polyanion interaction as non-core; the read abstract does not resolve every residue or prove all related glycosaminoglycans bind equivalently. Supporting Evidence: PMID:16233946 Heparin binding to human low density lipoproteins (LDL) |
| GO:0008203 cholesterol metabolic process | IMP PMID:2563166 Association between a specific apolipoprotein B mutation and... | ACCEPT | Summary: Retain the established broad scope with explicit source limits. Reason: The complete available PMID:2563166 abstract links a human apoB100 mutation to defective LDL-receptor binding and hypercholesterolemia. Retain the existing curated IMP cholesterol-metabolic-process assertion with that receptor-dependent cholesterol-handling scope and the full-text access limit. ApoB itself supplies the receptor-recognition surface as part of the lipid particle; this is not a claim that apoB catalyzes cholesterol synthesis or ester hydrolysis. GO:0008203 is a descendant of lipid metabolic process, so the broader existing row is treated consistently; transport alone is not used as a synonym for metabolism. Supporting Evidence: PMID:2563166 low density lipoproteins that bind defectively to the apoB,E(LDL) receptor. file:human/APOB/APOB-notes.md |
| GO:0009615 response to virus | IEP PMID:16548883 Transcriptomic and proteomic analyses of rhabdomyosarcoma ce... | KEEP AS NON CORE | Summary: Retain response to virus in the reported contextual role. Reason: The 16548883 abstract reports apoB transcript and protein changes after EV71 infection of rhabdomyosarcoma cells. Retain this directly observed expression response as non-core, without inferring an antiviral effector mechanism from induction. Supporting Evidence: PMID:16548883 Western blot analyses of APOB, CLU, DCAMKL1 and ODC1 proteins correlated protein and transcript levels. |
| GO:0010008 endosome membrane | TAS Reactome:R-HSA-171059 | KEEP AS NON CORE | Summary: Retain endosome membrane in the reported contextual role. Reason: R-HSA-171059 moves receptor-bound LDL from coated vesicles toward endosomes. Retain transient association with the endosomal receptor complex as a contextual non-core location, not a stable integral-membrane apoB topology. Supporting Evidence: Reactome:R-HSA-171059 |
| GO:0010008 endosome membrane | TAS Reactome:R-HSA-171106 | UNDECIDED | Summary: The source-specific endosome membrane assertion remains unresolved. Reason: R-HSA-171106 explicitly discusses LDL dissociation from LDLR in the early endosome and subsequent LDL lysosomal delivery. That supports luminal cargo but leaves the specific endosome-membrane association at this dissociation/recycling event uncertain; do not infer permanent membrane membership from LDLR's topology. |
| GO:0010744 positive regulation of macrophage derived foam cell differentiation | IDA PMID:17244792 Induction of dendritic cell-like phenotype in macrophages du... | UNDECIDED | Summary: The source-specific positive regulation of macrophage derived foam cell differentiation assertion remains unresolved. Reason: The complete available PMID:17244792 abstract describes macrophages exposed to LDL/modified LDL or infection-associated lipid loading. The original apoB-specific assay distinguishing active regulatory work from delivery of a lipid-rich particle has not been inspected. Preserve this experimental positive regulation of macrophage derived foam cell differentiation assertion as uncertain, not disproven by substrate reasoning or abstract silence. |
| GO:0010744 positive regulation of macrophage derived foam cell differentiation | IDA PMID:18322245 C-reactive protein-bound enzymatically modified low-density ... | UNDECIDED | Summary: The source-specific positive regulation of macrophage derived foam cell differentiation assertion remains unresolved. Reason: The complete available PMID:18322245 abstract describes macrophages exposed to LDL/modified LDL or infection-associated lipid loading. The original apoB-specific assay distinguishing active regulatory work from delivery of a lipid-rich particle has not been inspected. Preserve this experimental positive regulation of macrophage derived foam cell differentiation assertion as uncertain, not disproven by substrate reasoning or abstract silence. |
| GO:0010744 positive regulation of macrophage derived foam cell differentiation | IDA PMID:19114110 Chlamydia pneumoniae induces macrophage-derived foam cell fo... | UNDECIDED | Summary: The source-specific positive regulation of macrophage derived foam cell differentiation assertion remains unresolved. Reason: The complete available PMID:19114110 abstract describes macrophages exposed to LDL/modified LDL or infection-associated lipid loading. The original apoB-specific assay distinguishing active regulatory work from delivery of a lipid-rich particle has not been inspected. Preserve this experimental positive regulation of macrophage derived foam cell differentiation assertion as uncertain, not disproven by substrate reasoning or abstract silence. |
| GO:0010884 positive regulation of lipid storage | IDA PMID:18322245 C-reactive protein-bound enzymatically modified low-density ... | UNDECIDED | Summary: The source-specific positive regulation of lipid storage assertion remains unresolved. Reason: The complete available PMID:18322245 abstract describes macrophages exposed to LDL/modified LDL or infection-associated lipid loading. The original apoB-specific assay distinguishing active regulatory work from delivery of a lipid-rich particle has not been inspected. Preserve this experimental positive regulation of lipid storage assertion as uncertain, not disproven by substrate reasoning or abstract silence. |
| GO:0010886 positive regulation of cholesterol storage | IDA PMID:19114110 Chlamydia pneumoniae induces macrophage-derived foam cell fo... | UNDECIDED | Summary: The source-specific positive regulation of cholesterol storage assertion remains unresolved. Reason: The complete available PMID:19114110 abstract describes macrophages exposed to LDL/modified LDL or infection-associated lipid loading. The original apoB-specific assay distinguishing active regulatory work from delivery of a lipid-rich particle has not been inspected. Preserve this experimental positive regulation of cholesterol storage assertion as uncertain, not disproven by substrate reasoning or abstract silence. |
| GO:0030301 cholesterol transport | IBA GO_REF:0000033 | ACCEPT | Summary: Established cholesterol transport fits the principal apoB role. Reason: Cholesterol carriage is a defining apoB-particle role supported by human lipid/LDLR phenotypes and direct structural lipid association. Accept the PAINT process assertion on convergent human biology while leaving its uninspected tree reconstruction unstated; P04114 in WITH/FROM is valid experimental grounding, not circularity. Supporting Evidence: PMID:39662503 an approximately 61-nm-long continuous amphipathic Ξ²-sheet that wraps around the LDL particle like a belt. |
| GO:0030301 cholesterol transport | IMP PMID:15308631 Overexpression of human diacylglycerol acyltransferase 1, ac... | ACCEPT | Summary: Established cholesterol transport fits the principal apoB role. Reason: The 15308631 abstract reports increased secretion of apoB-containing VLDL after altering neutral-lipid synthesis in rat McA-RH7777 cells expressing human lipid enzymes. Preserve that species boundary; human apoB cholesterol carriage is independently established. Accept the clearly correct process without attributing the enzymes' cholesterol esterification chemistry to apoB. Supporting Evidence: PMID:15308631 These effects were associated with decreased intracellular degradation and increased secretion of newly synthesized apoB as VLDL. PMID:39662503 an approximately 61-nm-long continuous amphipathic Ξ²-sheet that wraps around the LDL particle like a belt. |
| GO:0030301 cholesterol transport | IMP PMID:2563166 Association between a specific apolipoprotein B mutation and... | ACCEPT | Summary: Established cholesterol transport fits the principal apoB role. Reason: Human 2563166 links an apoB receptor-binding mutation with defective LDL particles and hypercholesterolemia. ApoB physically carries cholesterol-containing particles and recognizes uptake receptors, supporting this transport role rather than a free-cholesterol transfer-pocket mechanism. Supporting Evidence: PMID:2563166 low density lipoproteins that bind defectively to the apoB,E(LDL) receptor. |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-171059 | KEEP AS NON CORE | Summary: Retain clathrin-coated endocytic vesicle membrane in the reported contextual role. Reason: The read Reactome:R-HSA-171059 summary describes transport of LDL:LDLR coated vesicles to endosomes. Retain transient receptor-complex association with coated-vesicle membrane as non-core. ApoB remains extracellular/luminal lipoprotein cargo, not a clathrin coat or membrane-spanning subunit. Supporting Evidence: Reactome:R-HSA-171059 |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-171141 | KEEP AS NON CORE | Summary: Retain clathrin-coated endocytic vesicle membrane in the reported contextual role. Reason: The read Reactome:R-HSA-171141 summary describes LDLR-dependent internalization of LDL. Retain transient receptor-complex association with coated-vesicle membrane as non-core. ApoB remains extracellular/luminal lipoprotein cargo, not a clathrin coat or membrane-spanning subunit. Supporting Evidence: Reactome:R-HSA-171141 |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-174706 | KEEP AS NON CORE | Summary: Retain clathrin-coated endocytic vesicle membrane in the reported contextual role. Reason: The read Reactome:R-HSA-174706 summary describes LDLR-dependent internalization of apoE-bearing remnants. Retain transient receptor-complex association with coated-vesicle membrane as non-core. ApoB remains extracellular/luminal lipoprotein cargo, not a clathrin coat or membrane-spanning subunit. Supporting Evidence: Reactome:R-HSA-174706 |
| GO:0031904 endosome lumen | TAS Reactome:R-HSA-171106 | KEEP AS NON CORE | Summary: Retain endosome lumen in the reported contextual role. Reason: R-HSA-171106 describes released LDL in the early-endosome lumen before lysosomal delivery. Retain the luminal cargo location as non-core; no endosomal catalytic or trafficking-machinery activity is assigned to apoB. Supporting Evidence: Reactome:R-HSA-171106 |
| GO:0031904 endosome lumen | TAS Reactome:R-HSA-8876366 | KEEP AS NON CORE | Summary: Retain endosome lumen in the reported contextual role. Reason: R-HSA-8876366 describes LDL movement from endosomes to lysosomes. Retain endosome-lumen presence as a transient cargo location rather than a principal functional compartment. Supporting Evidence: Reactome:R-HSA-8876366 |
| GO:0034359 mature chylomicron | IBA GO_REF:0000033 | ACCEPT | Summary: Established mature chylomicron fits the principal apoB role. Reason: ApoB48 is a structural constituent of intestinal chylomicrons, supported by human particle assays and the RNA-edited-product record. Accept the PAINT location; target self-evidence in WITH/FROM is legitimate. The exact ancestral tree has not been reconstructed. Supporting Evidence: PMID:4363408 Purified lymph and plasma chylomicrons and plasma very low density lipoproteins (VLDL) produced displacement curves in the assay system which paralleled those produced by pure LDL. |
| GO:0034359 mature chylomicron | IDA PMID:4363408 Assay of total plasma apolipoprotein B concentration in huma... | ACCEPT | Summary: Established mature chylomicron fits the principal apoB role. Reason: The 4363408 abstract directly quantifies apoB in purified human lymph/plasma chylomicrons by immunoassay. This supports its principal particle membership; the historical immunological comparison does not erase the later-established apoB48/apoB100 sequence distinction. Supporting Evidence: PMID:4363408 Purified lymph and plasma chylomicrons and plasma very low density lipoproteins (VLDL) produced displacement curves in the assay system which paralleled those produced by pure LDL. |
| GO:0034360 chylomicron remnant | TAS PMID:6099394 Plasma lipoproteins: apolipoprotein structure and function. | ACCEPT | Summary: Established chylomicron remnant fits the principal apoB role. Reason: The 6099394 review concerns apolipoprotein structure and lipoprotein metabolism; its abstract is broad. Chylomicron-remnant membership is independently consistent with the persistent apoB48 scaffold and the read remnant pathway records, so retain this clearly established location without claiming a new direct experiment in the review. Supporting Evidence: PMID:4363408 The assay measures not only the ApoB content of beta-lipoproteins (low density lipoproteins [LDL]) but also that contained in the other lipoproteins in plasma. |
| GO:0034361 very-low-density lipoprotein particle | IBA GO_REF:0000033 | ACCEPT | Summary: Established very-low-density lipoprotein particle fits the principal apoB role. Reason: ApoB100 is a principal structural protein of VLDL. Human particle assays and secretory-cell studies support the PAINT location independently; preserve the original donor list without treating target self-evidence as circular or claiming the unavailable tree was examined. Supporting Evidence: PMID:4363408 Purified lymph and plasma chylomicrons and plasma very low density lipoproteins (VLDL) produced displacement curves in the assay system which paralleled those produced by pure LDL. |
| GO:0034361 very-low-density lipoprotein particle | IDA PMID:15308631 Overexpression of human diacylglycerol acyltransferase 1, ac... | ACCEPT | Summary: Established very-low-density lipoprotein particle fits the principal apoB role. Reason: The 15308631 abstract measures secreted VLDL apoB in rat hepatoma cells expressing human lipid enzymes. That context is retained, while human VLDL apoB is independently directly established by 4363408. Accept the particle location without calling all reagents human. Supporting Evidence: PMID:15308631 These effects were associated with decreased intracellular degradation and increased secretion of newly synthesized apoB as VLDL. |
| GO:0034361 very-low-density lipoprotein particle | IDA PMID:4363408 Assay of total plasma apolipoprotein B concentration in huma... | ACCEPT | Summary: Established very-low-density lipoprotein particle fits the principal apoB role. Reason: The human plasma immunoassay in 4363408 directly measures apoB in purified VLDL, supporting principal VLDL particle membership. Supporting Evidence: PMID:4363408 The assay measures not only the ApoB content of beta-lipoproteins (low density lipoproteins [LDL]) but also that contained in the other lipoproteins in plasma. |
| GO:0034361 very-low-density lipoprotein particle | TAS PMID:27477018 TREM2 Binds to Apolipoproteins, Including APOE and CLU/APOJ,... | ACCEPT | Summary: Established very-low-density lipoprotein particle fits the principal apoB role. Reason: The 27477018 abstract describes lipoproteins as TREM2 ligands but does not expose the precise apoB assay. The TAS VLDL location is independently directly established by human particle measurements, so accept this clearly correct membership while keeping the TREM2-specific function separately unresolved. Supporting Evidence: PMID:4363408 Purified lymph and plasma chylomicrons and plasma very low density lipoproteins (VLDL) produced displacement curves in the assay system which paralleled those produced by pure LDL. |
| GO:0034362 low-density lipoprotein particle | IBA GO_REF:0000033 | ACCEPT | Summary: Established low-density lipoprotein particle fits the principal apoB role. Reason: ApoB100 is the defining structural protein on human LDL, directly demonstrated by human particle assays and the native LDL cryo-EM study 39662503. Accept this PAINT location without criticizing self-derived experimental support or claiming complete tree access. Supporting Evidence: PMID:39662503 an approximately 61-nm-long continuous amphipathic Ξ²-sheet that wraps around the LDL particle like a belt. |
| GO:0034362 low-density lipoprotein particle | IDA PMID:4363408 Assay of total plasma apolipoprotein B concentration in huma... | ACCEPT | Summary: Established low-density lipoprotein particle fits the principal apoB role. Reason: The human LDL preparation in 4363408 directly supports apoB membership, independently corroborated by the actual native human LDL structure 39662503. Supporting Evidence: PMID:4363408 The assay measures not only the ApoB content of beta-lipoproteins (low density lipoproteins [LDL]) but also that contained in the other lipoproteins in plasma. |
| GO:0034362 low-density lipoprotein particle | TAS PMID:27477018 TREM2 Binds to Apolipoproteins, Including APOE and CLU/APOJ,... | ACCEPT | Summary: Established low-density lipoprotein particle fits the principal apoB role. Reason: LDL apoB membership is directly established in human particle assays and the human LDL structure, independently of the unread detailed TREM2 assay in 27477018. Accept the TAS particle location, without extending that acceptance to every receptor-specific claim in the same paper. Supporting Evidence: PMID:39662503 an approximately 61-nm-long continuous amphipathic Ξ²-sheet that wraps around the LDL particle like a belt. |
| GO:0034363 intermediate-density lipoprotein particle | IDA PMID:1917954 Mechanisms of inhibition by apolipoprotein C of apolipoprote... | ACCEPT | Summary: Established intermediate-density lipoprotein particle fits the principal apoB role. Reason: The complete 1917954 abstract explicitly describes apoB100 and apoE in human plasma IDL and uses antibodies to distinguish their contributions to fibroblast-receptor interactions. Accept IDL particle membership as part of the apoB100 carrier continuum. Supporting Evidence: PMID:1917954 IDL is a lipoprotein that contains both apoB-100 and apoE. |
| GO:0034374 low-density lipoprotein particle remodeling | IMP PMID:15797858 Mutation in apolipoprotein B associated with hypobetalipopro... | UNDECIDED | Summary: The source-specific low-density lipoprotein particle remodeling assertion remains unresolved. Reason: The 15797858 abstract reports altered VLDL-to-LDL conversion and LDL turnover in human R3480P carriers, but the full experiments remain inaccessible. The official remodeling term concerns acquisition/loss/modification of particle protein or lipid; apoB's own structural contribution to that specific step cannot be resolved merely from altered turnover. Preserve the IMP assertion as uncertain rather than declaring the substrate incapable of participation. |
| GO:0034379 very-low-density lipoprotein particle assembly | IDA PMID:15308631 Overexpression of human diacylglycerol acyltransferase 1, ac... | ACCEPT | Summary: Established very-low-density lipoprotein particle assembly fits the principal apoB role. Reason: ApoB directly provides the lipid-binding structural scaffold needed to build VLDL, rather than being only an inert substrate. The 15308631 rat-cell lipid-enzyme experiments report apoB-particle assembly/secretion, while human MTP/export studies and structural evidence independently establish the conserved human role. No lipid-synthetic enzyme activity is attributed to apoB. Supporting Evidence: PMID:15308631 These effects were associated with decreased intracellular degradation and increased secretion of newly synthesized apoB as VLDL. |
| GO:0034383 low-density lipoprotein particle clearance | IMP PMID:15797858 Mutation in apolipoprotein B associated with hypobetalipopro... | ACCEPT | Summary: Established low-density lipoprotein particle clearance fits the principal apoB role. Reason: The human 15797858 abstract reports reduced mutant LDL receptor affinity and altered in-vivo turnover. ApoB100 itself performs the receptor-recognition step contributing to clearance. The production GO-CAM 632cf60a00000028 expressly connects apoB receptor binding to LDL clearance using this source; no receptor/adaptor machinery is assigned to apoB. Supporting Evidence: PMID:15797858 R3480P LDL bound with lower affinity to the LDL receptor than non-carrier LDL in vitro |
| GO:0034383 low-density lipoprotein particle clearance | IMP PMID:2563166 Association between a specific apolipoprotein B mutation and... | ACCEPT | Summary: Established low-density lipoprotein particle clearance fits the principal apoB role. Reason: The human 2563166 apoB mutation causes defective LDL receptor binding and hypercholesterolemia. ApoB receptor recognition directly contributes to clearance, supporting the process rather than relying solely on a downstream disease phenotype. Supporting Evidence: PMID:2563166 low density lipoproteins that bind defectively to the apoB,E(LDL) receptor. |
| GO:0035473 lipase binding | IPI PMID:9685400 Interaction between ApoB and hepatic lipase mediates the upt... | KEEP AS NON CORE | Summary: Retain lipase binding in the reported contextual role. Reason: The complete 9685400 abstract reports hepatic-lipase binding to apoB26/48/100, LDL-coated plate/ligand-blot controls and anti-apoB inhibition of enhanced LDL uptake. Retain the specific lipase interaction as non-core accessory recognition; apoB does not thereby acquire lipase catalytic activity. Supporting Evidence: PMID:9685400 On a ligand blot, HL bound to apoB26, 48, and 100 but not to apoE or apoAI. |
| GO:0042627 chylomicron | IDA PMID:4363408 Assay of total plasma apolipoprotein B concentration in huma... | ACCEPT | Summary: Established chylomicron fits the principal apoB role. Reason: The purified human chylomicron immunoassays in 4363408 directly support apoB particle membership. Preserve this general source assertion alongside the mature-chylomicron row without inventing a new duplicate annotation. Supporting Evidence: PMID:4363408 Purified lymph and plasma chylomicrons and plasma very low density lipoproteins (VLDL) produced displacement curves in the assay system which paralleled those produced by pure LDL. |
| GO:0042627 chylomicron | IDA PMID:8245722 Identification of disulfide-linked apolipoprotein species in... | ACCEPT | Summary: Established chylomicron fits the principal apoB role. Reason: The 8245722 abstract describes human lipoprotein fractions including chylomicrons, but the apoB100βapoAII result is specifically VLDL/LDL. General chylomicron apoB membership is directly established by independent human 4363408 and the apoB48 product record; retain the clearly correct location without misquoting this study as proving apoB100 in normal chylomicrons. Supporting Evidence: PMID:4363408 Purified lymph and plasma chylomicrons and plasma very low density lipoproteins (VLDL) produced displacement curves in the assay system which paralleled those produced by pure LDL. |
| GO:0042632 cholesterol homeostasis | IBA GO_REF:0000033 | ACCEPT | Summary: Established cholesterol homeostasis fits the principal apoB role. Reason: Human apoB receptor-binding defects and its structural lipid-carrier role directly connect it to cholesterol homeostasis. Accept the PAINT process on that convergent biology; do not treat P04114 in its own donor list as circular evidence. |
| GO:0042632 cholesterol homeostasis | IMP PMID:2563166 Association between a specific apolipoprotein B mutation and... | ACCEPT | Summary: Established cholesterol homeostasis fits the principal apoB role. Reason: The human 2563166 mutant apoB/defective-LDL phenotype directly connects apoB receptor recognition and lipid distribution with cholesterol homeostasis. This is consistent with the established molecular role and does not assign cholesterol synthesis to apoB. Supporting Evidence: PMID:2563166 low density lipoproteins that bind defectively to the apoB,E(LDL) receptor. |
| GO:0042953 lipoprotein transport | IBA GO_REF:0000033 | ACCEPT | Summary: Established lipoprotein transport fits the principal apoB role. Reason: ApoB remains physically associated with lipoprotein particles as their lipid-carrying scaffold and, for apoB100, receptor-recognition ligand. Those roles contribute to lipoprotein transport. Accept the PAINT process without claiming the unavailable ancestral tree was reconstructed. |
| GO:0043025 neuronal cell body | IDA PMID:22897442 Apolipoprotein B is a new target of the GDNF/RET and ET-3/ED... | UNDECIDED | Summary: The source-specific neuronal cell body assertion remains unresolved. Reason: The 22897442 abstract explicitly describes murine Neuro2a cells and mouse Ret-mutant embryos, but not the full neuronal-cell-body localization experiment. Preserve the human IDA as unresolved pending its original assay/species transfer context; do not call it a wrong-gene or wrong-species annotation from the abstract. |
| GO:0043202 lysosomal lumen | TAS Reactome:R-HSA-8865667 | KEEP AS NON CORE | Summary: Retain lysosomal lumen in the reported contextual role. Reason: R-HSA-8865667 places internalized LDL in the lysosomal lumen where LIPA hydrolyzes its cholesteryl esters. Retain apoB-containing cargo in this degradation compartment as non-core, with LIPA performing the chemistry. Supporting Evidence: Reactome:R-HSA-8865667 |
| GO:0043202 lysosomal lumen | TAS Reactome:R-HSA-8876366 | KEEP AS NON CORE | Summary: Retain lysosomal lumen in the reported contextual role. Reason: R-HSA-8876366 describes delivery of internalized LDL from endosomes to the lysosomal lumen. Retain the cargo destination as non-core and do not equate it with apoB lysosomal enzyme activity. Supporting Evidence: Reactome:R-HSA-8876366 |
| GO:0043231 intracellular membrane-bounded organelle | TAS PMID:7853698 [Apolipoprotein B]. | ACCEPT | Summary: Retain the established broad scope with explicit source limits. Reason: The broad organelle location is correct for apoB's independently demonstrated ER/secretory-pathway pool, including the human apoB cargo examined in PMID:27138255. Retain the existing assertion without changing its original TAS source. The full PMID:7853698 review remains uninspected and its abstract concerns RNA editing; that original source's precise localization argument is therefore not verified. The current do-not-annotate subset discourages such broad new annotations but does not make the existing location biologically false. No ER-specific replacement is manufactured from the uninspected original paper; the existing precise ER assertions and separate corroborating reference remain explicit. Supporting Evidence: PMID:27138255 TANGO1 binds TALI, and both interact with apolipoprotein B (ApoB) and are necessary for the recruitment of ApoB-containing lipid particles to ER exit sites for their subsequent export. file:human/APOB/APOB-notes.md |
| GO:0048018 receptor ligand activity | IDA PMID:27477018 TREM2 Binds to Apolipoproteins, Including APOE and CLU/APOJ,... | UNDECIDED | Summary: The source-specific receptor ligand activity assertion remains unresolved. Reason: The production GO-CAM 6606056e00001418 explicitly models human apoB as a TREM2-activating ligand with IDA27477018. The primary abstract reports lipoprotein/TREM2 recognition, but its apoB-specific reagent and activation panels remain unread. Preserve the experimental claim as unresolved in this audit, not as a rejected ligand role or a supposed curator omission. |
| GO:0050750 low-density lipoprotein particle receptor binding | IBA GO_REF:0000033 | ACCEPT | Summary: Established low-density lipoprotein particle receptor binding fits the principal apoB role. Reason: ApoB100 LDL-receptor recognition is directly supported by human defective-apoB studies, the isolated-site binding work and the receptor-complex structural abstract of PMID:39663455. Accept this PAINT MF; P04114 self-evidence is appropriate, and no donor-count objection or uninspected phylogenetic placement is asserted. |
| GO:0050750 low-density lipoprotein particle receptor binding | IMP PMID:15797858 Mutation in apolipoprotein B associated with hypobetalipopro... | ACCEPT | Summary: Established low-density lipoprotein particle receptor binding fits the principal apoB role. Reason: The 15797858 complete abstract explicitly reports lower LDLR affinity of human R3480P-carrier LDL than non-carrier LDL in vitro. This directly supports the existing receptor-binding claim, while full assay details and the distinct cholesterol-transfer claim remain separately unresolved. Supporting Evidence: PMID:15797858 R3480P LDL bound with lower affinity to the LDL receptor than non-carrier LDL in vitro |
| GO:0050750 low-density lipoprotein particle receptor binding | IMP PMID:2563166 Association between a specific apolipoprotein B mutation and... | ACCEPT | Summary: Established low-density lipoprotein particle receptor binding fits the principal apoB role. Reason: The 2563166 human familial-defective-apoB study links a specific apoB mutation with LDL particles that bind defectively to the LDL receptor. This is consistent with the independently established direct receptor-recognition role and supports the existing MF. Supporting Evidence: PMID:2563166 low density lipoproteins that bind defectively to the apoB,E(LDL) receptor. |
| GO:0050750 low-density lipoprotein particle receptor binding | IPI PMID:27477018 TREM2 Binds to Apolipoproteins, Including APOE and CLU/APOJ,... | UNDECIDED | Summary: The source-specific low-density lipoprotein particle receptor binding assertion remains unresolved. Reason: The original partner is TREM2. GO:0050750 describes binding to a low-density lipoprotein receptor and does not state that only the LDLR gene qualifies. The relevant PMID:27477018 apoB-specific binding assay has not been inspected, so retain uncertainty instead of rejecting the partner by name or replacing the assertion with evidence from a different LDLR paper. |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | MARK AS OVER ANNOTATED | Summary: Detected in an extracellular-vesicle proteome, but the detection does not establish that this protein is an EV constituent. Reason: Apolipoprotein B, which MISEV2018 (PMID:30637094) names as a negative marker. Here, exosomes from expressed prostatic secretions in urine: APOB-containing lipoproteins are large and are not normally filtered into urine, so this detection is more likely co-isolated plasma or seminal-fluid material than EV cargo. MISEV2018 category 3a covers non-EV structures that co-isolate with EVs, chiefly lipoproteins and albumin, from plasma, serum and serum-containing culture; detection does not establish EV localization. (Manual re-review for OMICS_EVIDENCE, 2026-10-10; previous action: UNDECIDED.) |
| GO:0070971 endoplasmic reticulum exit site | IDA PMID:27138255 TANGO1 and Mia2/cTAGE5 (TALI) cooperate to export bulky pre-... | KEEP AS NON CORE | Summary: Retain endoplasmic reticulum exit site in the reported contextual role. Reason: Actual27138255 Results/Methods show endogenous human apoB cargo recruitment to ER exit sites with TANGO1/TALI. Retain this export-cargo location as non-core relative to lipid carriage/particle assembly; apoB is not given the cargo receptor or coat adaptor activity. Supporting Evidence: PMID:27138255 TANGO1 binds TALI, and both interact with apolipoprotein B (ApoB) and are necessary for the recruitment of ApoB-containing lipid particles to ER exit sites for their subsequent export. |
| GO:0071402 cellular response to lipoprotein particle stimulus | IDA PMID:27477018 TREM2 Binds to Apolipoproteins, Including APOE and CLU/APOJ,... | UNDECIDED | Summary: The source-specific cellular response to lipoprotein particle stimulus assertion remains unresolved. Reason: The production TREM2 GO-CAM explicitly includes apoB ligand activity in this cellular response using 27477018. That is a considered curator assertion, not a gap or proof of substrate exclusion. The relevant apoB-specific activation/uptake experiment remains unread, so leave the existing process uncertain without manufacturing a new response term. |
| GO:0071682 endocytic vesicle lumen | TAS Reactome:R-HSA-2247511 | KEEP AS NON CORE | Summary: Retain endocytic vesicle lumen in the reported contextual role. Reason: The read Reactome:R-HSA-2247511 summary describes STAB2 internalizes ligand-containing complexes. Retain apoB-containing particle presence in the endocytic-vesicle lumen as non-core cargo localization, not as evidence that apoB performs membrane scission or receptor trafficking. Supporting Evidence: Reactome:R-HSA-2247511 |
| GO:0071682 endocytic vesicle lumen | TAS Reactome:R-HSA-2247512 | KEEP AS NON CORE | Summary: Retain endocytic vesicle lumen in the reported contextual role. Reason: The read Reactome:R-HSA-2247512 summary describes CD36 internalizes oxidized LDL. Retain apoB-containing particle presence in the endocytic-vesicle lumen as non-core cargo localization, not as evidence that apoB performs membrane scission or receptor trafficking. Supporting Evidence: Reactome:R-HSA-2247512 |
| GO:0071682 endocytic vesicle lumen | TAS Reactome:R-HSA-2247513 | KEEP AS NON CORE | Summary: Retain endocytic vesicle lumen in the reported contextual role. Reason: The read Reactome:R-HSA-2247513 summary describes STAB1 internalizes modified LDL. Retain apoB-containing particle presence in the endocytic-vesicle lumen as non-core cargo localization, not as evidence that apoB performs membrane scission or receptor trafficking. Supporting Evidence: Reactome:R-HSA-2247513 |
| GO:0071682 endocytic vesicle lumen | TAS Reactome:R-HSA-2247514 | KEEP AS NON CORE | Summary: Retain endocytic vesicle lumen in the reported contextual role. Reason: The read Reactome:R-HSA-2247514 summary describes SCARF1 internalizes modified LDL. Retain apoB-containing particle presence in the endocytic-vesicle lumen as non-core cargo localization, not as evidence that apoB performs membrane scission or receptor trafficking. Supporting Evidence: Reactome:R-HSA-2247514 |
| GO:0071682 endocytic vesicle lumen | TAS Reactome:R-HSA-2507854 | KEEP AS NON CORE | Summary: Retain endocytic vesicle lumen in the reported contextual role. Reason: The read Reactome:R-HSA-2507854 summary describes MSR1 internalizes modified LDL. Retain apoB-containing particle presence in the endocytic-vesicle lumen as non-core cargo localization, not as evidence that apoB performs membrane scission or receptor trafficking. Supporting Evidence: Reactome:R-HSA-2507854 |
| GO:0071682 endocytic vesicle lumen | TAS Reactome:R-HSA-2512800 | KEEP AS NON CORE | Summary: Retain endocytic vesicle lumen in the reported contextual role. Reason: R-HSA-2512800 explicitly includes SR-BI-mediated endocytosis of oxidized LDL, inferred from mouse studies, alongside human partial endocytic contribution to selective lipid uptake. Thus the available event supports a transient endocytic particle-cargo pool; it is not limited to selective transfer of lipids without the particle. Retain this cargo location as non-core while preserving the mouse-inference and human selective-uptake distinctions; it does not make apoB an endocytic enzyme or coat component. Supporting Evidence: Reactome:R-HSA-2512800 |
| GO:0071682 endocytic vesicle lumen | TAS Reactome:R-HSA-2981040 | UNDECIDED | Summary: The source-specific endocytic vesicle lumen assertion remains unresolved. Reason: R-HSA-2981040 principally describes COLEC12-dependent yeast/bacterial uptake and extends the model to other ligands. The apoB-specific endocytic cargo/entity evidence has not been inspected, so the exact vesicle-lumen assertion remains uncertain. |
| GO:0120020 cholesterol transfer activity | IBA GO_REF:0000033 | UNDECIDED | Summary: The source-specific cholesterol transfer activity assertion remains unresolved. Reason: The official GO:0120020 definition specifies cholesterol extraction and protected aqueous delivery, not merely carriage in a lipoprotein. The source-linked human IMP annotation from PMID:15797858 full experiment and PTN002673834 node/MSA remain unavailable after bounded access attempts. Retain the IBA as uncertain without calling target self-evidence circular or using donor count as a proxy for validity. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN002673834 UNRESOLVED The GOA node identifier was inspected, but its IBD assertion, tree placement and MSA were not recovered in the bounded configured PAINT attempt. No donor-count or self-evidence objection is asserted. |
| GO:0120020 cholesterol transfer activity | IMP PMID:15797858 Mutation in apolipoprotein B associated with hypobetalipopro... | UNDECIDED | Summary: The source-specific cholesterol transfer activity assertion remains unresolved. Reason: The accessible PMID:15797858 abstract addresses human apoB mutation effects on LDLR affinity and VLDL/LDL turnover; the full assay supporting the narrower cholesterol-transfer MF could not be checked. Preserve this experimental assertion as uncertain rather than inferring that no such experiment exists or replacing it from abstract silence. |
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Download this section (compressed HTML)Q: Which source-specific assay establishes extraction and protected aqueous transfer of cholesterol by apoB, distinct from carriage inside a lipoprotein particle?
Q: What APOB construct and ligand/activation experiments underlie the curated TREM2 activities, and how do these differ from the LDLR recognition interfaces?
Q: Does the plasma-membrane label retained on nested LDL:LDLR entities after Reactome vesicle scission intentionally encode persistent surface association, or should it follow the outer complex to the endocytic-vesicle compartment?
Q: Which apoB-specific perturbations distinguish direct regulatory work in foam-cell formation from delivery of the lipid-rich particle?
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