Ceruloplasmin is a secreted multicopper glycoprotein whose ferroxidase activity oxidizes Fe(II) to Fe(III), coupling extracellular iron handling to cellular iron homeostasis. Soluble plasma ceruloplasmin and membrane-associated forms provide different spatial contexts for this chemistry. Loss of ceruloplasmin causes tissue iron accumulation in aceruloplasminemia. Additional measured activities include glutathione-dependent peroxide reduction, cuprous-ion oxidation and inhibition of myeloperoxidase; stressed plasma ceruloplasmin also associates with the extracellular chaperone clusterin.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004322 ferroxidase activity | EXP PMID:10481051 Glutathione peroxidase-like activity of caeruloplasmin as an... | ACCEPT | Summary: Ceruloplasmin has experimentally supported ferroxidase activity. Reason: PMID:10481051 describes ferroxidase alongside peroxide reduction. The primary ferroxidase role is independently supported by human enzyme replacement in PMID:29183916. Retention respects the experimental curation; the older paper was available only as an abstract, so its detailed iron assay was not independently reconstructed. |
| GO:0004322 ferroxidase activity | EXP PMID:5912351 The possible significance of the ferrous oxidase activity of... | ACCEPT | Summary: The historical serum-ferroxidase annotation represents the established catalytic function. Reason: PMID:5912351 is authenticated by title and bibliographic metadata, but no abstract or full original was recovered. Retain the well-established EXP assertion with curator deference and independent human CP evidence in PMID:29183916; the 1966 experimental protocol remains unverified. |
| GO:0004322 ferroxidase activity | IDA PMID:14623105 Cuprous oxidase activity of yeast Fet3p and human ceruloplas... | ACCEPT | Summary: Human ceruloplasmin oxidizes ferrous iron. Reason: The PMID:14623105 abstract explicitly includes human ceruloplasmin and the ferroxidase reaction. Its shared-site kinetic analysis is described for yeast Fet3p and is not assigned to human CP. The human activity is retained without claiming that the inaccessible full paper was read. |
| GO:0004322 ferroxidase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The combined electronic mapping identifies the specific ferroxidase reaction. Reason: RHEA:11148 and EC:1.16.3.1 match the reaction recorded for human CP. Mouse Q61147 has a current same-term IDA record from PMID:16436657 as well as inferred records; independent human experiments support this conserved activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q61147 SUPPORTS TRANSFER Exact CP ferroxidase reaction in reviewed human record; mouse same-term IDA from PMID:16436657 is present. This is a literal current donor-record reference, not an independently read primary paper. ensembl:ENSMUSP00000088857 SUPPORTS TRANSFER Original Ensembl mouse product identifier retained; UniProt Q61147 supplies the inspected mouse annotation context. RHEA:11148 SUPPORTS TRANSFER Listed combined-mapping premise; RHEA:11148 / EC:1.16.3.1 identify Fe(II) oxidation. EC:1.16.3.1 SUPPORTS TRANSFER Listed combined-mapping premise; RHEA:11148 / EC:1.16.3.1 identify Fe(II) oxidation. |
| GO:0004322 ferroxidase activity | IMP PMID:16150804 Functional relevance of ceruloplasmin mutations in Parkinson... | ACCEPT | Summary: Human ceruloplasmin variants alter serum ferroxidase activity. Reason: The PMID:16150804 abstract reports reduced serum ferroxidase activity and impaired holoprotein production for defined variants. These observations support the normal enzyme activity; mutant GPI-construct retention in the ER is not normal functional localization. Full Methods and exact human GPI sequence mapping remain unavailable. |
| GO:0004322 ferroxidase activity | IMP PMID:29183916 Ceruloplasmin replacement therapy ameliorates neurological s... | ACCEPT | Summary: Human soluble ceruloplasmin restores ferroxidase activity in Cp-deficient mice. Reason: PMID:29183916 uses purified human soluble CP administered to Cp-knockout mice and measures restored brain ferroxidase activity. This supports human protein catalysis in the tested treatment context, without establishing universal brain entry or equivalent activity of every alternative product. Supporting Evidence: PMID:29183916 rescue of ferroxidase activity |
| GO:0004322 ferroxidase activity | TAS PMID:7708681 Aceruloplasminemia: molecular characterization of this disor... | ACCEPT | Summary: Human aceruloplasminemia supports the physiological ferroxidase role. Reason: PMID:7708681 links a truncating human CP defect to absence of circulating CP and excess tissue iron. This TAS row is consistent with established catalytic evidence, while the genetic study itself is not presented as a newly inspected purified-enzyme assay. |
| GO:0004322 ferroxidase activity | TAS Reactome:R-HSA-917891 | ACCEPT | Summary: Reactome assigns iron oxidation to the CP-containing extracellular complex. Reason: R-HSA-917891 explicitly describes CP-dependent Fe(II) oxidation. The saved catalyst-to-complex-to-CP path reaches UniProt:P00450. CP performs the oxidation; the associated transporter SLC40A1 performs membrane transport. |
| GO:0004602 glutathione peroxidase activity | IDA PMID:10481051 Glutathione peroxidase-like activity of caeruloplasmin as an... | KEEP AS NON CORE | Summary: Ceruloplasmin reduces hydrogen peroxide in the presence of glutathione. Reason: The PMID:10481051 abstract directly reports H2O2 removal with physiological reduced-glutathione concentrations, matching GO:0004602. Retain this secondary activity alongside the dominant ferroxidase role; detailed kinetics and product context await the original full paper. Supporting Evidence: PMID:10481051 Cp can remove both hydrogen peroxide and lipid hydroperoxides |
| GO:0004602 glutathione peroxidase activity | IDA PMID:10508415 Ceruloplasmin has a distinct active site for the catalyzing ... | UNDECIDED | Summary: The alkyl-hydroperoxide study supports peroxidase activity, but the exact H2O2 assay remains unresolved. Reason: PMID:10508415 explicitly reports human CP alkyl-hydroperoxide reduction and a cysteinyl-site perturbation. GO:0004602 names the H2O2 reaction. Because the original Methods were not recovered, the specific substrate underlying this IDA assertion cannot be independently distinguished from the reported organic-peroxide activity. Preserve the annotation pending that source check. |
| GO:0004602 glutathione peroxidase activity | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: The reaction mapping supports a secondary glutathione-peroxidase activity. Reason: GO_REF:0000120 combines RHEA:16833 and EC:1.11.1.9, the H2O2/glutathione reaction recorded in reviewed human CP. PMID:10481051 explicitly supports that substrate pair. This is a positive ancillary activity, not a reason to replace the ferroxidase core. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: RHEA:16833 SUPPORTS TRANSFER The curated reaction specifies glutathione and H2O2; PMID:10481051 provides independent substrate support. EC:1.11.1.9 SUPPORTS TRANSFER The curated reaction specifies glutathione and H2O2; PMID:10481051 provides independent substrate support. |
| GO:0005507 copper ion binding | IEA GO_REF:0000120 | ACCEPT | Summary: Copper binding supplies the metal cofactor for ceruloplasmin catalysis. Reason: The InterPro multicopper-oxidase domains and mouse copper-binding records agree with the human CP copper centers. The reviewed human record and structures support six copper cations per monomer. Cofactor binding is integrated with the ferroxidase core rather than made a separate biological role. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q61147 SUPPORTS TRANSFER Inspected multicopper-oxidase domain or mouse cofactor-binding premise; human CP structures independently establish the copper sites. ensembl:ENSMUSP00000088857 SUPPORTS TRANSFER Inspected multicopper-oxidase domain or mouse cofactor-binding premise; human CP structures independently establish the copper sites. InterPro:IPR002355 SUPPORTS TRANSFER Inspected multicopper-oxidase domain or mouse cofactor-binding premise; human CP structures independently establish the copper sites. InterPro:IPR011706 SUPPORTS TRANSFER Inspected multicopper-oxidase domain or mouse cofactor-binding premise; human CP structures independently establish the copper sites. InterPro:IPR011707 SUPPORTS TRANSFER Inspected multicopper-oxidase domain or mouse cofactor-binding premise; human CP structures independently establish the copper sites. |
| GO:0005576 extracellular region | HDA PMID:16502470 Human colostrum: identification of minor proteins in the aqu... | ACCEPT | Summary: Soluble ceruloplasmin is an extracellular protein. Reason: The human-colostrum proteomics study PMID:16502470 is compatible with secreted CP. Its CP-specific table was not recovered, so this retention rests on established soluble extracellular biology and curator deference, not a claimed independent target-row validation. |
| GO:0005576 extracellular region | HDA PMID:20551380 Proteomics characterization of extracellular space component... | ACCEPT | Summary: Human aortic NaCl extracts contain ceruloplasmin. Reason: The actual Table I CERU_HUMAN row in PMID:20551380 reports four unique peptides, four unique spectra, 2.3% coverage and nine total spectra. The caption identifies three NaCl extracts, not the separate guanidine or SDS fractions. This supports extracellular detection without proving a structural matrix role. Supporting Evidence: PMID:20551380 Extracellular space proteins identified by proteomics in three NaCl extracts |
| GO:0005576 extracellular region | IDA PMID:16150804 Functional relevance of ceruloplasmin mutations in Parkinson... | ACCEPT | Summary: Normal soluble ceruloplasmin is secreted into serum. Reason: PMID:16150804 measures serum CP concentration and ferroxidase activity. Its mutant GPI-linked construct retained in the ER is a separate abnormal trafficking observation and does not redefine the normal soluble product location. |
| GO:0005576 extracellular region | IDA PMID:19996109 Identification of human plasma proteins as major clients for... | ACCEPT | Summary: The clusterin study directly detects human ceruloplasmin in plasma. Reason: PMID:19996109 uses human plasma and identifies CP among clusterin-associated proteins after prolonged physiological-temperature shear stress. This establishes extracellular presence independently of the source-specific chaperone-binding interpretation. |
| GO:0005576 extracellular region | IEA GO_REF:0000120 | ACCEPT | Summary: The electronic extracellular-region annotation fits soluble CP secretion. Reason: The combined location mapping is consistent with soluble extracellular CP. None of the 280 current ARBA00027128 branches matches the official target signatures and taxonomy; this does not establish the historical rule version or negate independent evidence for soluble secretion. The annotation does not assign extracellular-region location to the cell-surface-attached product. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00027128 UNRESOLVED All 280 current branches were evaluated against official target identities, including five FunFam signatures, and taxonomy; no current branch matches. Historical rule-version applicability remains unresolved, while independent evidence supports soluble CP secretion. UniProtKB:Q61147 SUPPORTS TRANSFER Soluble secretion is independently established; SL-0243 is a location vocabulary mapping, not a donor experiment. ensembl:ENSMUSP00000088857 SUPPORTS TRANSFER Soluble secretion is independently established; SL-0243 is a location vocabulary mapping, not a donor experiment. UniProtKB-SubCell:SL-0243 SUPPORTS TRANSFER Soluble secretion is independently established; SL-0243 is a location vocabulary mapping, not a donor experiment. |
| GO:0005576 extracellular region | NAS PMID:14718574 The human plasma proteome: a nonredundant list developed by ... | ACCEPT | Summary: The plasma-proteome source is consistent with soluble extracellular ceruloplasmin. Reason: PMID:14718574 combines plasma-proteome datasets, but the original CP row was not independently recovered. Retain the NAS at established soluble-protein location, corroborated by the directly inspected human-plasma work in PMID:19996109. |
| GO:0005576 extracellular region | TAS PMID:7708681 Aceruloplasminemia: molecular characterization of this disor... | ACCEPT | Summary: Circulating serum ceruloplasmin has extracellular location. Reason: PMID:7708681 describes loss of circulating serum CP in human aceruloplasminemia. The soluble circulating product is the scope of this location annotation, distinct from membrane-associated CP. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5621402 | ACCEPT | Summary: Reactome records an extracellular CP component in this iron-handling event. Reason: R-HSA-5621402: The disease reaction contains extracellular CP mutant entities inside a CP:copper:SLC40A1 complex. Its failed oxidation describes mutant function, not evidence that normal CP lacks activity. The retained annotation follows the explicitly recorded CP component location; it is not a blanket location assignment to every GPI-anchored product. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655733 | ACCEPT | Summary: Reactome records an extracellular CP component in this iron-handling event. Reason: R-HSA-5655733: The disease reaction contains normal extracellular CP as a component of a mutant-SLC40A1 complex. Failed iron transport belongs to the transporter defect, not loss of normal CP secretion. The retained annotation follows the explicitly recorded CP component location; it is not a blanket location assignment to every GPI-anchored product. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-904830 | ACCEPT | Summary: Reactome records an extracellular CP component in this iron-handling event. Reason: R-HSA-904830: The transport reaction contains an extracellular CP component in the SLC40A1 complex. CP supports iron handling without itself becoming the transmembrane transporter. The retained annotation follows the explicitly recorded CP component location; it is not a blanket location assignment to every GPI-anchored product. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-917891 | ACCEPT | Summary: Reactome records an extracellular CP component in this iron-handling event. Reason: R-HSA-917891: The oxidation reaction contains extracellular CP as the ferroxidase component of the SLC40A1 complex. The retained annotation follows the explicitly recorded CP component location; it is not a blanket location assignment to every GPI-anchored product. |
| GO:0005765 lysosomal membrane | HDA PMID:17897319 Integral and associated lysosomal membrane proteins. | UNDECIDED | Summary: The lysosomal-membrane proteomics assertion remains source-specific and unresolved. Reason: PMID:17897319 surveyed human placental lysosomal membranes. Its abstract does not identify CP, and the original target table and membrane-association evidence were not recovered. This prevents a confident source-specific judgment; neither the secreted nature of CP nor the absence of the target in the abstract disproves the annotation. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-8952289 | KEEP AS NON CORE | Summary: Ceruloplasmin is present in the ER lumen during secretory-pathway processing. Reason: R-HSA-8952289 explicitly includes CP in the FAM20C substrate and phosphorylated-product sets in the ER lumen. The reconstructed input/output paths support this transit location. FAM20C performs phosphorylation; this does not imply CP is a kinase or that its main ferroxidase activity occurs in the ER. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Membrane-associated ceruloplasmin supports the plasma-membrane IBA. Reason: The current v19 CP leaf lies below PANTHER:PTN000194708. Its aligned sequence differs from the current official product at residue 544, which is recorded without claiming exact sequence equality. Mammalian GPI-associated CP evidence supports this product context; human numbered splice accessions and activity equivalence are not inferred. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000194708 SUPPORTS TRANSFER Current v19 target PTN002542383 descends from this node. MSA D544/current E544 difference is recorded; the membrane-associated product context is retained. |
| GO:0006878 intracellular copper ion homeostasis | IDA PMID:14623105 Cuprous oxidase activity of yeast Fet3p and human ceruloplas... | UNDECIDED | Summary: Cuprous-ion oxidation is positive, while the cellular copper-homeostasis assertion needs the full source. Reason: The PMID:14623105 abstract establishes cuprous oxidase activity for human CP and proposes a homeostatic role. GO:0006878 concerns maintenance of intracellular copper levels. With the original full text inaccessible, a cellular homeostasis experiment cannot be confirmed or excluded. Preserve the IDA assertion and the positive chemistry without converting this access limit into a negative function claim. |
| GO:0006879 intracellular iron ion homeostasis | IDA PMID:14623105 Cuprous oxidase activity of yeast Fet3p and human ceruloplas... | ACCEPT | Summary: Ferroxidase chemistry directly supports cellular iron homeostasis. Reason: PMID:14623105 identifies human CP as a ferroxidase associated with iron homeostasis. Extracellular oxidation of iron is part of maintaining cellular iron balance, not merely a disease correlation. The paper-specific kinetic-site evidence described for yeast is not transposed to human CP. |
| GO:0006879 intracellular iron ion homeostasis | IMP PMID:16150804 Functional relevance of ceruloplasmin mutations in Parkinson... | ACCEPT | Summary: Altered human CP activity affects iron homeostasis. Reason: PMID:16150804 combines serum enzyme measurements and variant-associated holoprotein/trafficking defects. This supports the iron-homeostasis role at the tested human variant context; it does not establish all variants or products as functionally equivalent. |
| GO:0006879 intracellular iron ion homeostasis | IMP PMID:29183916 Ceruloplasmin replacement therapy ameliorates neurological s... | ACCEPT | Summary: Human CP replacement reduces iron accumulation in the Cp-knockout model. Reason: PMID:29183916 measures restored ferroxidase activity and reduced brain iron deposition after human soluble CP administration. The enzyme directly changes iron oxidation state, so this process annotation is supported by performed chemistry as well as the rescue phenotype. Supporting Evidence: PMID:29183916 reduced brain iron deposition |
| GO:0006879 intracellular iron ion homeostasis | TAS PMID:9445478 Role of ceruloplasmin in cellular iron uptake. | ACCEPT | Summary: Ceruloplasmin modulates cellular iron uptake in human HepG2 cells. Reason: The PMID:9445478 abstract reports increased iron uptake and altered apparent affinity in HepG2 cells, with iron-dependent CP expression. Retain that uptake context; it should not be rewritten as exclusively iron efflux. Full experimental details remain unavailable. |
| GO:0006879 intracellular iron ion homeostasis | TAS Reactome:R-HSA-917937 | ACCEPT | Summary: CP performs a ferroxidase step within the iron-homeostasis pathway. Reason: R-HSA-917937 contains the CP-specific oxidation and associated iron-export reactions. Typed paths connect the pathway through those events to P00450. The supported role is CP redox chemistry, not an inferred claim that CP executes every transport step. |
| GO:0016491 oxidoreductase activity | IBA GO_REF:0000033 | MODIFY | Summary: Ferroxidase activity specifies the principal oxidoreductase function. Reason: PANTHER:PTN000194698 supports a broad redox category. The current target lies below the cited ancestral node; a one-residue current-MSA difference is documented. This is a specificity refinement, not a rejection of PAINT or a donor-count argument. Human enzyme and iron-homeostasis evidence justify GO:0004322 as the specific retained function. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: PANTHER:PTN000194698 SUPPORTS TRANSFER The current target descends from this broad redox node; target self-evidence and donor count do not invalidate it. Human ferroxidase is the chosen more specific function. Proposed replacements: ferroxidase activity |
| GO:0016491 oxidoreductase activity | IEA GO_REF:0000002 | MODIFY | Summary: Ferroxidase activity specifies the principal oxidoreductase function. Reason: InterPro:IPR011706 supports a broad redox category. The multicopper-oxidase domain mapping is biologically valid but does not identify the physiological substrate on its own. Human enzyme and iron-homeostasis evidence justify GO:0004322 as the specific retained function. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: InterPro:IPR011706 SUPPORTS TRANSFER The multicopper-oxidase mapping supports redox chemistry; primary human data resolve the ferroxidase substrate. Proposed replacements: ferroxidase activity |
| GO:0016722 oxidoreductase activity, acting on metal ions | IEA GO_REF:0000117 | MODIFY | Summary: Ferroxidase activity specifies the principal oxidoreductase function. Reason: Current ARBA00027769 branch 7 matches the official CP FunFam signatures 2.60.40.420:FF:000009 and 2.60.40.420:FF:000015 together with the Primates taxon predicate. This supports the broad metal-ion oxidoreductase premise. Human enzyme and iron-homeostasis evidence identify ferroxidase activity as the specific principal function, so GO:0004322 is the replacement. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: ARBA:ARBA00027769 SUPPORTS TRANSFER All 14 current branches were evaluated against official target signatures and taxonomy. Branch 7 matches both FunFam signatures and Primates (NCBITaxon:9443). This current match supports the broad premise without reproducing a historical rule version. Proposed replacements: ferroxidase activity |
| GO:0016724 oxidoreductase activity, acting on metal ions, oxygen as acceptor | IDA PMID:14623105 Cuprous oxidase activity of yeast Fet3p and human ceruloplas... | KEEP AS NON CORE | Summary: The experimental metal-ion oxidoreductase category includes the reported cuprous activity. Reason: PMID:14623105 explicitly reports human CP oxidation of Cu(I) as well as Fe(II). Retain this broader oxygen-acceptor category for the additional cuprous substrate scope. Replacing it solely with ferroxidase would erase that positive experimental distinction; the current typed children expose only ferroxidase, not a verified cuprous-specific child. |
| GO:0036479 peroxidase inhibitor activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ceruloplasmin directly inhibits myeloperoxidase. Reason: The Ensembl Compara source Q61147 has current IDA PMID:23306200 for this term. The same original also directly tests human plasma-purified CP binding to and inhibiting MPO, with kinetic evidence for trapping Compound II. This is a real secondary activity, distinct from the dominant ferroxidase role. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q61147 SUPPORTS TRANSFER Current mouse Q61147 same-term IDA from PMID:23306200 is present; that paper also tests purified human CP inhibition directly. ensembl:ENSMUSP00000088857 SUPPORTS TRANSFER Original mouse Ensembl premise retained; no PAINT method is inferred for this orthology mapping. Supporting Evidence: PMID:23306200 binding of ceruloplasmin to myeloperoxidase inhibits the halogenation activity |
| GO:0036479 peroxidase inhibitor activity | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Ceruloplasmin directly inhibits myeloperoxidase. Reason: The manual orthology source Q61147 has current IDA PMID:23306200 for this term. The same original also directly tests human plasma-purified CP binding to and inhibiting MPO, with kinetic evidence for trapping Compound II. This is a real secondary activity, distinct from the dominant ferroxidase role. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q61147 SUPPORTS TRANSFER Current mouse Q61147 same-term IDA from PMID:23306200 is present; that paper also tests purified human CP inhibition directly. |
| GO:0047066 phospholipid-hydroperoxide glutathione peroxidase activity | IDA PMID:10481051 Glutathione peroxidase-like activity of caeruloplasmin as an... | KEEP AS NON CORE | Summary: The source reports glutathione-dependent removal of lipid hydroperoxides. Reason: PMID:10481051 explicitly describes lipid-hydroperoxide removal at physiological glutathione concentrations. Retain this experimentally curated secondary activity with that substrate scope. The inaccessible detailed Methods limit independent reconstruction of each lipid substrate and kinetic condition. |
| GO:0047066 phospholipid-hydroperoxide glutathione peroxidase activity | IDA PMID:10508415 Ceruloplasmin has a distinct active site for the catalyzing ... | UNDECIDED | Summary: The exact lipid substrate supporting this peroxidase IDA remains unresolved. Reason: PMID:10508415 reports human CP alkyl-hydroperoxide reduction, whereas GO:0047066 specifies a hydroperoxy polyunsaturated fatty acid. The inaccessible original Methods may contain the relevant substrate assay; the abstract alone neither verifies it nor refutes the curator. Preserve the annotation pending the source-specific check. |
| GO:0051087 protein-folding chaperone binding | IPI PMID:19996109 Identification of human plasma proteins as major clients for... | KEEP AS NON CORE | Summary: Stressed human plasma ceruloplasmin associates with clusterin. Reason: Original PMID:19996109 identifies CP as a stress-dependent clusterin client by immunoaffinity/MS, immunoblotting and controlled sandwich ELISA. GO:0051087 describes binding to a folding chaperone; it does not require the bound client to perform chaperone activity. Retain this positive IPI as non-core client binding, with CP fragmentation and ten-day plasma stress limiting intact-product and native-condition claims. No CP folding activity or participation in a protein-folding process is inferred. Supporting Evidence: PMID:19996109 These proteins were identified by mass spectrometry as ceruloplasmin, fibrinogen, and albumin. |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: Urinary exosome proteomics detects ceruloplasmin. Reason: The original NHLBI database row for CP/NP_000087 reports six peptides and reference 2, the PMID:19056867 study. Actual Methods define the urinary vesicle fraction and permit splice-shared peptides from one gene. Retain gene-level vesicle association without inferring isoform-specific cargo activity. |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | UNDECIDED | Summary: The EPS-urine exosome annotation awaits an inspectable CP target row. Reason: PMID:23533145 establishes the vesicle-proteomics design, but available supplement responses are HTML errors rather than a usable workbook. The CP-specific peptides and grouping could not be checked. This access limitation does not demonstrate that the curated detection is false. |
| GO:0072562 blood microparticle | HDA PMID:22516433 Proteomic analysis of microvesicles from plasma of healthy d... | UNDECIDED | Summary: The plasma microparticle detection remains unresolved at the target-row level. Reason: The PMID:22516433 abstract describes proteomics of sub-220-nm plasma vesicles. The retrieved supplement is an XML error, not a data table, so the CP identity/grouping cannot be independently inspected. Retain the source assertion pending access rather than reject it because CP is abundant in plasma. |
| GO:0098869 cellular oxidant detoxification | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Ceruloplasmin can contribute to oxidant detoxification. Reason: The historical mouse source resolves to Q61147. Its current same-term record is electronic, which does not reconstruct the earlier curator evidence. Independent human CP peroxide-removal activity in PMID:10481051 supports direct detoxification chemistry. Retain this secondary process without equating extracellular location with inability to protect cells. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: MGI:MGI:88476 SOURCE WEAK OR INFERRED Official cross-reference resolves to Q61147. Current same-term evidence is IEA, not a reconstruction or disproof of the historical ISS premise; human peroxide chemistry independently supports retention. |
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Download this section (compressed HTML)Q: Which complete human transcripts and processed protein sequences correspond to soluble and GPI-associated ceruloplasmin, and how does the GEYP-containing transcript relate to those products?
Q: Does human CP cuprous-ion oxidation measurably maintain intracellular copper levels under physiological conditions, independently of iron homeostasis?
Q: What are the CP peptide identities and protein-group assignments in the original lysosomal, EPS-urine and plasma-microparticle datasets?
Experiment: Compare sequence-verified human soluble and GPI-associated CP in matched expression systems, measuring secretion or surface attachment, copper loading, ferroxidase kinetics and iron export with equivalent protein amounts.
Experiment: Test purified human CP with defined H2O2 and phospholipid-hydroperoxide substrates, glutathione titrations and copper-loaded, apo and Cys-site controls to separate substrate scope from iron oxidation.
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