GANAB is the catalytic alpha subunit of the ER-lumen glucosidase II heterodimer with PRKCSH. It removes the two inner glucose residues from immature N-linked glycans, coupling glycan maturation to the calnexin/calreticulin folding cycle. Its glycan-processing activity supports maturation and trafficking of client glycoproteins, including polycystin-1 and polycystin-2. Pathogenic GANAB variants cause cystic kidney and liver disease.
Definition: Catalysis of the reaction: a monoglucosylated Glc1Man9GlcNAc2-protein + H2O = a Man9GlcNAc2-protein + D-glucose, removing the remaining glucose residue from the high-mannose N-linked glycan.
Justification: Human glucosidase II complexes hydrolyze both Glc1 and Glc2 substrates in PMID:10929008. The current GO:0106407 definition describes only Glc2-to-Glc1 hydrolysis, yet the production FlyBase GO-CAM 680ad14200001222 types two Gcs2alpha (FB:FBgn0027588) activities, 680ad14200001292 and 680ad14200001231, as GO:0106407 and links them by RO:0002413. Both enabled_by assertions use human UniProtKB:Q14697 as their ISS source. Their placement between glucosidase I and mannosidase, together with the primary chemistry, supports interpreting them as the successive inner-glucose removals; the model does not explicitly encode the intermediate glycans. The local dmel_n_glycan_processing module likewise uses GO:0106407 for both removals, and projects/GLYCOBIOLOGY/cazy2go.generated.terms.yaml records the ec2go-derived EC:3.2.1.207-to-GO:0106407 mapping. The latter is a retained generated mapping, not a newly retrieved ec2go release. RHEA:56000 also crossreferences GO:0106407 for the final-glucose reaction. These positive usage records supersede a null ontology search as the basis for reconciliation. The preferred resolution is to reconcile or broaden the existing term definition to cover its documented two-step usage, preserving the current model and module typing. This NTR remains conditional: if curators retain the Glc2-only definition and create a separate final-glucose term, the downstream GO-CAM activity and the final-step representation within the combined module would need specific retyping; the Glc2 activity should retain GO:0106407. The definition uses D-glucose because the inspected human assays do not establish product-anomer stereochemistry. RHEA beta-D-glucose and the retaining GH31 mechanism warrant an explicit question, not an asserted source defect. GO:0015926 remains the conservative generic parent; the actual GO:0106407 is_a GO:0090599 edge is acknowledged despite their conflicting product wording. The original HPLC substrates had the reported GlcNAc1 reducing end; the glycoprotein GlcNAc2 representation follows the curated reaction. No incoming evidence field or new original annotation is introduced.
Parent term: glucosidase activity
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | KEEP AS NON CORE | Summary: GANAB was recovered in the human HeLa mRNA-contact proteome (PMID:22658674). Reason: Original Table S1 contains GANAB/ENSG00000089597 among significant interactome proteins after UV crosslinking and stringent oligo(dT) purification. The assay supports RNA contact, rather than a protein co-immunoprecipitation alone. It does not identify a GANAB RNA target, regulatory mechanism, or natural splice product, and GANAB-specific GFP validation was not inspected. Retain this contextual activity outside the glycan-trimming core. The significant-list inclusion is supported by the ion-count route, whereas the DESeq comparison gives adjusted P=0.930; the target also appears in whole-cell lysate. GANAB has a signal peptide and a mature ER-lumen location, so this experiment does not establish how it encounters RNA in intact cells. These method and topology limits do not by themselves prove an abundance artifact or a false-positive identification. Supporting Evidence: PMID:22658674 covalent UV crosslinking of RBPs to RNA file:human/GANAB/GANAB-external-evidence.md |
| GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds | IEA GO_REF:0000002 | MODIFY | Summary: The glycoside-hydrolase assignment can be specified to the demonstrated Glc2 N-glycan reaction. Reason: The InterPro IPR000322 assignment recognizes the glycosyl-hydrolase architecture. Human GANAB-containing glucosidase II directly removes glucose from Glc2Man9-containing glycans in PMID:10929008. GO:0106407 is the defined Glc2-to-Glc1 oligosaccharide reaction and is more informative than the broad O-glycosyl hydrolase term. The same human complexes also cleave the remaining glucose from the monoglucosylated glycan in PMID:10929008. That final-glucose reaction is represented by a conditional proposed term corresponding to RHEA:56000. Reconciliation of the existing GO:0106407 definition with its documented two-step usage is preferred; the separate proposal is retained for consideration if curators instead preserve the current Glc2-only definition. |
| GO:0005515 protein binding | IPI PMID:10929008 The heterodimeric structure of glucosidase II is required fo... | MODIFY | Summary: GANAB forms the catalytic alpha/beta glucosidase II heterodimer with PRKCSH. Reason: PMID:10929008 directly characterizes the human alpha/beta association, reconstitution, solubility and retention of glucosidase II. The explicit PRKCSH partner is the non-identical beta subunit, supporting protein heterodimerization rather than an uninformative generic protein-binding annotation. Single-human-subunit baculovirus preparations could associate with insect subunits, so those preparations are not treated as isolated human alpha monomers. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:10929008 the coexpression of the beta subunit |
| GO:0030246 carbohydrate binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Carbohydrate recognition is consistent with GANAB glycan-substrate engagement. Reason: The IPR011013-based carbohydrate-binding inference is compatible with the carbohydrate-recognition architecture and the experimentally established engagement of glucosylated N-glycan substrates. Retain this ancillary binding facet without inferring a separate extracellular lectin or carbohydrate-signaling role. The defining function is catalytic hydrolysis, represented by the substrate-specific activity in the core. |
| GO:0033919 glucan 1,3-alpha-glucosidase activity | IBA GO_REF:0000033 | MODIFY | Summary: The conserved glucosidase II activity is retained with the correct oligosaccharide substrate term. Reason: The current official GO:0033919 definition describes terminal cleavage in alpha-1,3-glucan polymers. The human assays in PMID:10929008 instead characterize glucosylated high-mannose oligosaccharides, including Glc2-to-Glc1 cleavage, which GO:0106407 names explicitly. Replace the term by that demonstrated chemistry. This is a substrate-based lateral correction between sibling activities, not a claim that GO:0106407 is its descendant or that conserved GANAB catalysis has been lost. The actual target AN77 descends from the PTN002734202/AN68 assertion; catalytic D542/D618 are conserved, and target self-evidence is legitimate. The phylogenetic placement remains supported while the transferred term is corrected. The same human complexes also cleave the remaining glucose from the monoglucosylated glycan in PMID:10929008. That final-glucose reaction is represented by a conditional proposed term corresponding to RHEA:56000. Reconciliation of the existing GO:0106407 definition with its documented two-step usage is preferred; the separate proposal is retained for consideration if curators instead preserve the current Glc2-only definition. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: PANTHER:PTN002734202 SUPPORTS TRANSFER Actual IBD and target tree path support inherited glucosidase II chemistry. Human and mouse experimental descendants ground the node; the correction concerns the polymer-versus-N-glycan substrate definition, not lineage loss or donor count. |
| GO:0033919 glucan 1,3-alpha-glucosidase activity | IEA GO_REF:0000120 | MODIFY | Summary: The electronic glucan-hydrolase mapping should name the observed Glc2 N-glycan reaction. Reason: The current official GO:0033919 definition describes terminal cleavage in alpha-1,3-glucan polymers. The human assays in PMID:10929008 instead characterize glucosylated high-mannose oligosaccharides, including Glc2-to-Glc1 cleavage, which GO:0106407 names explicitly. Replace the term by that demonstrated chemistry. This is a substrate-based lateral correction between sibling activities, not a claim that GO:0106407 is its descendant or that conserved GANAB catalysis has been lost. The same human complexes also cleave the remaining glucose from the monoglucosylated glycan in PMID:10929008. That final-glucose reaction is represented by a conditional proposed term corresponding to RHEA:56000. Reconciliation of the existing GO:0106407 definition with its documented two-step usage is preferred; the separate proposal is retained for consideration if curators instead preserve the current Glc2-only definition. |
| GO:0033919 glucan 1,3-alpha-glucosidase activity | IDA PMID:10929008 The heterodimeric structure of glucosidase II is required fo... | MODIFY | Summary: The original human enzyme experiment supports oligosaccharide trimming, not the polymer definition. Reason: The current official GO:0033919 definition describes terminal cleavage in alpha-1,3-glucan polymers. The human assays in PMID:10929008 instead characterize glucosylated high-mannose oligosaccharides, including Glc2-to-Glc1 cleavage, which GO:0106407 names explicitly. Replace the term by that demonstrated chemistry. This is a substrate-based lateral correction between sibling activities, not a claim that GO:0106407 is its descendant or that conserved GANAB catalysis has been lost. Both tested long human alpha forms were active with beta on the natural Glc1/Glc2 substrates; no Glc3 cleavage was detected under the reported assay conditions. The same human complexes also cleave the remaining glucose from the monoglucosylated glycan in PMID:10929008. That final-glucose reaction is represented by a conditional proposed term corresponding to RHEA:56000. Reconciliation of the existing GO:0106407 definition with its documented two-step usage is preferred; the separate proposal is retained for consideration if curators instead preserve the current Glc2-only definition. Proposed replacements: Glc2Man9GlcNAc2 oligosaccharide glucosidase activity Glc1Man9GlcNAc2 oligosaccharide glucosidase activity Supporting Evidence: |
| GO:0090599 alpha-glucosidase activity | IDA PMID:28375157 Isolated polycystic liver disease genes define effectors of ... | MODIFY | Summary: GANAB alpha-glucosidase activity has an established N-glycan substrate specificity. Reason: The 2017 PCLD study supports GANAB-dependent protein biogenesis and the curated activity assertion; its exact activity experiment was not recovered independently from the abstract-only cache and failed original routes. Independent human enzyme experiments in PMID:10929008 directly establish the specific Glc2 N-glycan reaction. Refine the broad alpha-glucosidase term to GO:0106407 on that combined evidence, without claiming the inaccessible experiment was erroneous or that every alpha-glucoside is a physiological substrate. The same human complexes also cleave the remaining glucose from the monoglucosylated glycan in PMID:10929008. That final-glucose reaction is represented by a conditional proposed term corresponding to RHEA:56000. Reconciliation of the existing GO:0106407 definition with its documented two-step usage is preferred; the separate proposal is retained for consideration if curators instead preserve the current Glc2-only definition. The actual ontology has GO:0106407 is_a GO:0090599, so this is a refinement in the current graph. The conflicting alpha/beta product wording is an unresolved definition/reaction issue, not evidence that this typed edge is absent or that GANAB has lost alpha-glucosidase chemistry. |
| GO:0106407 Glc2Man9GlcNAc2 oligosaccharide glucosidase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The electronic annotation names the demonstrated Glc2-to-Glc1 N-glycan reaction. Reason: The official current GO:0106407 definition specifies hydrolysis of the diglucosylated high-mannose N-glycan to its monoglucosylated form. Human glucosidase II assays in PMID:10929008 directly support this reaction. Preserve the incoming machine label, while using the current official label in authored synthesis. The same enzyme also removes the remaining glucose, but that second transition is not included in this GO definition. |
| GO:0106407 Glc2Man9GlcNAc2 oligosaccharide glucosidase activity | IDA PMID:10929008 The heterodimeric structure of glucosidase II is required fo... | ACCEPT | Summary: Human GANAB-containing glucosidase II directly cleaves the Glc2 glycan substrate. Reason: Selected original Results and HPLC substrate experiments in PMID:10929008 show activity of both tested human alpha splice forms with beta on Glc2 and Glc1 high-mannose oligosaccharides. The Glc2 transition directly supports GO:0106407. The natural assay substrates had the reported reducing-end GlcNAc composition; this supports the glucosidase II reaction without pretending the experiment measured every glycoprotein substrate or that GO:0106407 covers both transitions. Supporting Evidence: |
| GO:0005975 carbohydrate metabolic process | IEA GO_REF:0000002 | MODIFY | Summary: The broad carbohydrate process can be specified to ER N-glycan trimming. Reason: GANAB performs the hydrolytic glucose-removal step itself, as established by the human enzyme experiments and normal glucosidase II reaction model. This is direct participation in endoplasmic-reticulum N-glycan trimming, rather than passive necessity for a client protein. GO:0140277 specifies the conserved process more accurately than general carbohydrate metabolism. Proposed replacements: endoplasmic reticulum N-glycan trimming |
| GO:0006491 N-glycan processing | IBA GO_REF:0000033 | MODIFY | Summary: The ancestral N-glycan-processing function is conserved and can be specified to ER trimming. Reason: Human GANAB directly performs the early glucose-trimming reactions of N-glycan processing. The actual eukaryotic PTN000509742/AN3 IBD, donor records and target AN77 descent support the transfer, with conserved catalytic residues and no target-path loss assertion. Refine the parent process to its verified child GO:0140277; no defect is inferred from the number of donors or the target appearing among them. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000509742 SUPPORTS TRANSFER The verified eukaryotic IBD and target descent support N-glycan processing; direct human chemistry resolves the more specific ER-trimming child. Proposed replacements: endoplasmic reticulum N-glycan trimming |
| GO:0006491 N-glycan processing | IEA GO_REF:0000120 | MODIFY | Summary: The electronic N-glycan-processing annotation can name the directly performed ER trimming step. Reason: The electronic assertion is biologically sound but broader than the characterized reaction. GANAB catalyzes glucose removal from immature N-glycans in ER glucosidase II, supporting the is_a child GO:0140277. This does not add later Golgi diversification or glycoprotein destination processes simply because GANAB is needed for client maturation. Proposed replacements: endoplasmic reticulum N-glycan trimming |
| GO:0006491 N-glycan processing | IDA PMID:10929008 The heterodimeric structure of glucosidase II is required fo... | MODIFY | Summary: The ComplexPortal human IDA record supports the specific ER N-glycan trimming process. Reason: The human enzyme experiments establish catalytic cleavage of the two inner glucose residues in the glucosidase II pathway. The ComplexPortal IDA record supports direct ER N-glycan trimming, specified by GO:0140277, and is retained alongside the distinct UniProt record from the same paper. Proposed replacements: endoplasmic reticulum N-glycan trimming Supporting Evidence: |
| GO:0006491 N-glycan processing | IDA PMID:10929008 The heterodimeric structure of glucosidase II is required fo... | MODIFY | Summary: The UniProt human IDA record supports the same ER N-glycan trimming process. Reason: PMID:10929008 supports direct GANAB-catalyzed ER glycan trimming. GO:0140277 gives this process specificity without adding an unsupported client-specific process. This UniProt IDA record is retained alongside the distinct ComplexPortal record based on the same human enzyme study. Proposed replacements: endoplasmic reticulum N-glycan trimming Supporting Evidence: |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000044 | ACCEPT | Summary: Endoplasmic-reticulum residence is a supported central location of GANAB. Reason: The UniProt location mapping is grounded in human GANAB localization and glucosidase II retention. The current original 33097077 WT expression/localization results and HPA record support ER residence. Retain the informative root-organelle claim beside the separate ER-lumen annotations; it is not replaced merely because the lumen is known. |
| GO:0005783 endoplasmic reticulum | IDA GO_REF:0000052 | ACCEPT | Summary: HPA antibody imaging supports human GANAB localization to the ER. Reason: The official HPA subcellular record reports supported ER staining with HPA061426 in MCF-7, Rh30 and U2OS cells, and ER staining in serum-starved hTERT-RPE1 cells. This is positive antibody-based localization, consistent with independent human GANAB experiments. It does not alone resolve lumen topology or splice-product specificity; keep the root ER term. |
| GO:0005783 endoplasmic reticulum | EXP PMID:33097077 Novel GANAB variants associated with polycystic liver diseas... | ACCEPT | Summary: Wild-type human GANAB shows the expected ER-associated distribution. Reason: Selected original Results/Figure4 caption and Methods in PMID:33097077 describe N-terminal FLAG human GANAB, HEK293/HeLa expression and confocal localization with GIIbeta/PDI reagents. WT GANAB colocalized with GIIbeta in the HeLa system. Aberrant nuclear or diffuse patterns of engineered disease mutants are not assigned to normal splice products. Retain ER residence without claiming that the assay resolves the lumen independently. Supporting Evidence: |
| GO:0005788 endoplasmic reticulum lumen | NAS PMID:10929008 The heterodimeric structure of glucosidase II is required fo... | ACCEPT | Summary: GANAB acts in the lumenal glucosidase II complex. Reason: Human glucosidase II activity, subunit association and retention experiments support lumenal N-glycan processing. In the original study, modification of the beta-subunit HDEL retention signal produced secreted active enzyme, linking complex retention to the ER pathway. This annotation is retained at its literal NAS code while independent direct biology and the normal Reactome participant chain corroborate the location. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-532667 | ACCEPT | Summary: The normal second-glucose reaction explicitly contains lumenal GANAB. Reason: Reactome R-HSA-532667 names glucosidase II complex R-HSA-532671 as catalyst. Its component R-HSA-532674 is human UniProt Q14697, chain 29–944, in the ER lumen. The target membership is exact, and the location agrees with human enzyme evidence. The old catalyst GO:0033919 mapping in the model is not reused to override current substrate-specific ontology definitions. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-548890 | ACCEPT | Summary: The final-glucose reaction retains GANAB in the ER-lumen catalyst complex. Reason: The actual R-HSA-548890 participant record names glucosidase II R-HSA-532671 as catalyst of glucose removal/release from the chaperone-associated glycoprotein. Its Q14697 component is explicitly lumenal. This supports the location and the second hydrolytic transition; it does not make the Glc2-specific GO:0106407 definition cover that second transition. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-9683663 | ACCEPT | Summary: The SARS-CoV model uses the same lumenal human glucosidase II component. Reason: R-HSA-9683663 is an uncertain reaction model of Spike glycan trimming. Its ER-alpha-glucosidase set R-HSA-9682983 includes glucosidase II, whose component chain reaches Q14697. Thus the actual human participant has ER-lumen location. Retain this location using the verified chain and independent human GANAB evidence, without treating the viral model as a new target-specific infection experiment. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-9686790 | ACCEPT | Summary: The inhibitor-binding model preserves GANAB-containing glucosidase II in the ER lumen. Reason: R-HSA-9686790 has the ER-alpha-glucosidase set as an input and its inhibitor-bound counterpart as output. The set contains glucosidase II and ultimately the explicit human Q14697 lumenal component. This is a valid location attribution; it does not establish selective inhibition of GANAB over MOGS or a distinct antiviral biological function. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-9694364 | ACCEPT | Summary: The SARS-CoV-2 glycan model includes lumenal human GANAB through its catalyst set. Reason: The uncertain R-HSA-9694364 reaction names ER alpha-glucosidases and separately MOGS. The actual set-to-complex-to-Q14697 chain supports GANAB membership in the lumenal enzyme system. Preserve the location while keeping modeled Spike processing distinct from a directly read GANAB-specific infection assay. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-9932352 | ACCEPT | Summary: The CDH1 Glc2-processing model places GANAB in the ER-lumen catalyst. Reason: R-HSA-9932352 explicitly models the glucosidase II complex acting on glycosylated membrane CDH1, and the enzyme complex contains lumenal Q14697. The record states that CDH1 processing by glucosidase II has not been specifically studied, although the expected glycoform is detected. Retain the established enzyme location without transferring the membrane location of its substrate or inventing a new adhesion function. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-9932913 | ACCEPT | Summary: The CDH1 final-glucose model retains the same lumenal GANAB component. Reason: R-HSA-9932913 contains glucosidase II as catalyst of the modeled final glucose-removal step. The explicit Q14697 component remains ER lumen, whereas CDH1 and CANX are membrane-associated clients/partners. The event is labeled uncertain and lacks a specific glucosidase II–CDH1 assay; independent human glucosidase II evidence supports this location without overextending the client-specific model. |
| GO:0005794 Golgi apparatus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Pig ortholog evidence supports a nonexclusive post-ER/Golgi location. Reason: The exact donor P79403 is Sus scrofa GANAB, not a bovine or human record. Its official ER and Golgi annotations carry direct PMID:2404989 evidence; the authentic source abstract describes kidney tubular post-Golgi/brush-border distribution and active processed forms. This supports retaining the human ISS location as a contextual inference alongside predominant ER residence, without presenting it as a direct human assay or importing the donor reverse-ISS melanosome claim. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P79403 SUPPORTS TRANSFER Official pig GANAB record traces Golgi location directly to PMID:2404989. The abstract supports a post-Golgi distribution, while species identity comes from the curated donor record; direct human Golgi imaging was not read. |
| GO:0005794 Golgi apparatus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: The UniProt Golgi mapping is retained as contextual localization. Reason: The human UniProt Golgi statement is explicitly a similarity inference from pig GANAB P79403, whose direct location evidence is PMID:2404989, assessed in the reference list. It is compatible with an ER enzyme also occupying the secretory route and does not contradict the central lumenal ER function. Retain the organelle claim as non-core rather than replacing it by the ER or claiming direct human Golgi evidence. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | UNDECIDED | Summary: The precise GANAB membrane-fraction assignment remains unverified. Reason: PMID:19946888 profiled YTS-cell membrane preparations and includes attached/transient proteins as well as predicted integral membrane proteins. The cache is abstract-only and retained attempted supplementary spreadsheets are HTML error pages, so the exact GANAB identification and its association cannot be independently checked. GO:0016020 includes attached proteins, so lack of a transmembrane segment or known ER-lumen function is not evidence against the annotation. Retain uncertainty about this source-specific claim rather than remove it or assert an integral membrane topology. Supporting Evidence: |
| GO:0042470 melanosome | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: The electronic melanosome location reflects an actual GANAB fraction-proteomics observation. Reason: The underlying PMID:17081065 supplementary table explicitly lists Q14697/GANAB among proteins common to the tested melanosome stages. The human UniProt statement maps that mass-spectrometry evidence, not an independent localization experiment. Retain the contextual fraction association without inferring a melanin-synthesis activity, precise membrane topology, or splice-product specificity. |
| GO:0042470 melanosome | EXP PMID:17081065 Proteomic and bioinformatic characterization of the biogenes... | KEEP AS NON CORE | Summary: GANAB was identified in staged human melanosome preparations. Reason: The authentic ACS supplementary PDF for PMID:17081065 contains Q14697/GANAB in Supplemental Table 2, common proteins across the tested melanosome stages; Table 1 defines the MNT1/SK-MEL-28 gradient fractions. This positively verifies the target occurrence. It does not resolve GANAB orientation or demonstrate a catalytic role in melanogenesis, and co-fractionating secretory-system material remains a limitation. |
| GO:0043231 intracellular membrane-bounded organelle | IMP PMID:10929008 The heterodimeric structure of glucosidase II is required fo... | MODIFY | Summary: The broad intracellular-organelle localization can be specified to ER lumen. Reason: The source experiments concern the human glucosidase II complex and its beta-subunit retention signal, with active secretion after retention-signal replacement. Together with the verified Q14697 participant in normal ER-lumen reactions, this supports the more informative ER-lumen location. The general intracellular membrane-bounded organelle term is not one of the protected informative root-organelle terms. Proposed replacements: endoplasmic reticulum lumen |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: GANAB was detected in the urinary extracellular-vesicle fraction. Reason: The retained expanded NHLBI target table has GANAB-associated historical NP_938148 and NP_938149 rows, each with one peptide and reference 2 corresponding to PMID:19056867. The positive fraction detection is retained with the original urine extension. Historical isoform labels and accessions do not establish modern product specificity without peptide mapping, and no GANAB membrane orientation or vesicle-biogenesis activity is inferred. |
| GO:0070062 extracellular exosome | HDA PMID:19199708 Proteomic analysis of human parotid gland exosomes by multid... | KEEP AS NON CORE | Summary: GANAB was identified in the human parotid-saliva vesicle preparation. Reason: The authentic PMID:19199708 supplementary Paratid Exosomes sheet contains GANAB/IPI00383581.3 with 67 sequence identifications, 368 spectra, 57.6% coverage and a 944-residue entry. Selected original isolation and MS methods support a positive vesicle-enriched fraction observation, with potential co-isolated material remaining possible. Preserve the saliva extension; do not convert the historical entry into exclusive current-isoform localization or a secretion/vesicle-biogenesis function. |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | KEEP AS NON CORE | Summary: GANAB occurs in the noncancer urinary-vesicle proteomic pools. Reason: Original Supplemental Table 2 of PMID:23533145 contains Q14697/GANAB with 6 and 5 unique peptides in the two noncancer pools and 0 in the prostate-cancer pools. This supports urinary-vesicle-fraction detection under the reported preparation/MS conditions, not a general absence in cancer or a cancer-specific role. The preparation and common co-isolated proteins limit topology claims; no particular natural splice product is established. |
| GO:0017177 glucosidase II complex | IBA GO_REF:0000033 | ACCEPT | Summary: GANAB is the inherited catalytic alpha component of glucosidase II. Reason: The actual PTN002734202/AN68 IBD places glucosidase II complex membership in the clade containing human AN77/Q14697. The target sequence is exact and the human self-source is legitimate descendant experimental evidence. Original human alpha/beta experiments independently establish the heterodimer; there is no target-specific loss or discordant tree placement. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002734202 SUPPORTS TRANSFER The actual ancestral assertion, target descent and experimental descendant records support complex membership; the human self-source is expected, not circular. |
| GO:0017177 glucosidase II complex | IEA GO_REF:0000120 | ACCEPT | Summary: The electronic complex annotation agrees with directly established human glucosidase II. Reason: The electronic inference matches the human GANAB–PRKCSH alpha/beta complex characterized in PMID:10929008 and the exact normal Reactome component chain. This is a central complex membership, not an interaction-derived guess of an unrelated pathway role. |
| GO:0017177 glucosidase II complex | IDA PMID:10929008 The heterodimeric structure of glucosidase II is required fo... | ACCEPT | Summary: The human enzyme study directly establishes GANAB membership in glucosidase II. Reason: PMID:10929008 tests recombinant human alpha and beta subunits, their association and reconstituted glycan-cleaving activity. Both characterized long alpha splice products form the functional enzyme with beta. This supports complex membership; single-subunit insect-cell preparations that can recruit insect partners do not establish a physiologically isolated human alpha enzyme. Supporting Evidence: |
| GO:0017177 glucosidase II complex | IPI PMID:10929008 The heterodimeric structure of glucosidase II is required fo... | ACCEPT | Summary: The observed alpha/beta interaction supports the defined glucosidase II complex. Reason: The source interaction is between catalytic GANAB and regulatory/retention subunit PRKCSH within a characterized functional heterodimer, with activity and solubility/retention experiments in the same study. Retain the complex term at the literal IPI evidence code. The interaction is not treated merely as generic binding or as proof that every short predicted GANAB product assembles. Supporting Evidence: |
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Download this section (compressed HTML)Q: What N-glycan clients beyond the studied polycystins are most sensitive to partial GANAB loss in relevant human tissues?
Q: Does the very short Q14697-3 transcript produce a stable natural protein, and if so does it have any independent function?
Q: Which GANAB RNA contacts and vesicle/melanosome associations persist with target-specific validation and controls for secretory-system co-isolation?
Q: How should the product-anomer representation in RHEA:55996/RHEA:56000 and GO:0106407 be reconciled with the retaining GH31 mechanism and the alpha-D-glucose wording of GO:0090599? The inspected human GANAB assays establish glucose removal but do not independently resolve product-anomer stereochemistry.
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