GEMIN5 encodes a 1,508-residue RNA-binding protein that helps select small nuclear RNAs for assembly into spliceosomal ribonucleoproteins. Its N-terminal region forms two seven-bladed WD-repeat propellers with distinct surfaces for Sm-site RNA recognition and 7-methylguanosine-cap binding. As a peripheral component of the SMN assembly machinery, GEMIN5 links RNA recognition to delivery and assembly in the cytoplasm; nuclear pools occur in the nucleoplasm and gems. GEMIN5 also regulates translation through RNA and ribosome interactions. The direction of this regulation depends on the transcript and experimental context: SMN mRNA translation can be promoted, whereas global protein synthesis is restrained under other tested conditions. C-terminal RNA-binding regions provide additional recognition capacity. Biallelic damaging variants impair assembly-system function and cause neurodevelopmental disease.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000340 RNA 7-methylguanosine cap binding | IDA PMID:19750007 Identification of gemin5 as a novel 7-methylguanosine cap-bi... | ACCEPT | Summary: GEMIN5 binds the methylguanosine cap. Reason: The original human protein experiments support cap recognition. Their historical residue model is separate from the positive binding result; later structural evidence refines that model. |
| GO:0000340 RNA 7-methylguanosine cap binding | IDA PMID:27881600 Structural insights into Gemin5-guided selection of pre-snRN... | ACCEPT | Summary: GEMIN5 directly recognizes a methylguanosine cap. Reason: Purified human residues 1–739 bind the cap by ITC and resolve its recognition pocket structurally. Cellular mutant experiments distinguish cap-dependent recognition of truncated U1 RNA from the proposed downstream disposal route. Supporting Evidence: |
| GO:0000340 RNA 7-methylguanosine cap binding | IDA PMID:27881601 Structural basis for snRNA recognition by the double-WD40 re... | ACCEPT | Summary: The N-terminal domain directly binds the RNA cap. Reason: The human 1–726 construct and cap-bound structure support this activity. Its short-RNA competition model is assay-specific and does not negate the positive cap-binding result or establish universal competition with every snRNA. Supporting Evidence: |
| GO:0000387 spliceosomal snRNP assembly | EXP PMID:12067652 The SMN complex, an assemblyosome of ribonucleoproteins. | ACCEPT | Summary: GEMIN5 performs RNA-recognition work in snRNP assembly. Reason: The incoming ComplexPortal EXP assertion and review citation are preserved. Direct human RNA-binding and assembly experiments independently establish participation in this process; the cited 2002 review is not represented as a new GEMIN5-specific depletion experiment. |
| GO:0000387 spliceosomal snRNP assembly | IBA GO_REF:0000033 | ACCEPT | Summary: Spliceosomal snRNP assembly is an inherited core function. Reason: The exact 1508-residue target lies below the actual AN0/PTN005299808 assertion. Direct human recognition and assembly experiments support the node-derived function; no target-specific loss is demonstrated. |
| GO:0000387 spliceosomal snRNP assembly | IDA PMID:18984161 An assembly chaperone collaborates with the SMN complex to g... | ACCEPT | Summary: GEMIN5 participates in the cellular snRNP assembly machinery. Reason: The source tests the endogenous Gemin5-containing complex alongside simplified complexes lacking Gemins 3–5 or 3–7. Their activity limits claims of universal necessity, not the independently demonstrated RNA-recognition work of GEMIN5 in assembly. |
| GO:0000387 spliceosomal snRNP assembly | TAS PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | ACCEPT | Summary: GEMIN5 contributes directly to spliceosomal snRNP assembly. Reason: The discovery paper establishes Sm/SMN associations and proposes assembly participation. Later recognition and assembly experiments supply direct functional support, so the claim is retained without relabeling the original work as a depletion assay. |
| GO:0000398 mRNA splicing, via spliceosome | TAS PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | TOO GENERAL | Summary: The splicing claim is represented more precisely by snRNP assembly. Reason: GO:0000387 is explicitly part_of GO:0000398. Retained assembly annotations capture GEMIN5’s demonstrated contribution; the discovery source does not directly assay intron removal. This is specificity, not denial of the broader process. |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | MODIFY | Summary: The broad RNA annotation can be refined to mRNA binding. Reason: The incoming human HeLa mRNA-interactome assertion is retained, without claiming that the target table was independently recovered here. Direct human SMN-mRNA binding provides independent support for the more informative mRNA class; the verified is_a path places mRNA binding beneath RNA binding. The poly(A)-RNA screen supports the mRNA class independently of the separately retained SMN 3′-UTR assay; its unidentified captured sites are not assigned to 3′ UTRs. Proposed replacements: mRNA binding Supporting Evidence: PMID:25911097 Gemin5 binds to the mature, polyadenylated SMN 3′-UTR construct |
| GO:0003723 RNA binding | IPI PMID:34424823 The RBS1 domain of Gemin5 is intrinsically unstructured and ... | MODIFY | Summary: The tested viral IRES interaction supports mRNA 5′-UTR binding. Reason: Purified RBS1 fragments bind FMDV IRES d5/d5ss RNA. The original substrate study places this IRES domain upstream of the initiator codon, supporting the more specific mRNA 5′-UTR binding term. RNAcentral identifies the literal partner as a 462-nucleotide FMDV type-C IRES; this does not equate that complete record with either short assay reagent. The positive viral-substrate result is retained without generalizing it to endogenous targets or treating engineered RBS1 fragments as natural isoforms. Proposed replacements: mRNA 5'-UTR binding Supporting Evidence: PMID:34424823 the protein interacts with both RNAs to a similar extent PMID:23221641 interacting with the most 3′ end domain of the IRES element, upstream of the initiator codon |
| GO:0003730 mRNA 3'-UTR binding | IBA GO_REF:0000033 | ACCEPT | Summary: The inherited mRNA 3′-UTR-binding function has direct human support. Reason: The exact target descends from the asserted PAINT node AN0/PTN005299808. Human SMN-UTR binding independently supports the inherited claim; the target among the experimental donors is legitimate. |
| GO:0003730 mRNA 3'-UTR binding | IDA PMID:25911097 Gemin5 Binds to the Survival Motor Neuron mRNA to Regulate S... | ACCEPT | Summary: GEMIN5 directly recognizes the SMN mRNA 3′-UTR. Reason: Stringent purification, cellular crosslinking and sequence/structure perturbation support direct 3′-UTR recognition. This is a performed RNA-binding function; SMN-free and complex-associated protein pools are distinguished. Supporting Evidence: |
| GO:0003730 mRNA 3'-UTR binding | IEA GO_REF:0000117 | ACCEPT | Summary: The ARBA assignment agrees with demonstrated SMN 3′-UTR recognition. Reason: Human endogenous-protein and RNA-mutant experiments support this specific RNA-binding activity. The electronic rule is corroborated by those experiments, without treating the rule itself as an assay. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | REMOVE | Summary: The GEMIN2 association is retained as evidence. Reason: The reported complex association is positive evidence, although the isolated-protein assay differs. GEMIN2 organizes Sm assembly; that role does not establish the protein-folding chaperone class in GO:0051087. Generic protein binding adds no informative function. Supporting Evidence: UniProtKB:O14893 GEMIN2 constrains the conformation of 5Sm |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | REMOVE | Summary: GEMIN5 directly interacts with SmB. Reason: The purified-protein result is retained. SmB is an snRNP structural subunit; binding that subunit does not establish binding to a complete RNA–protein particle. The generic annotation is uninformative, not a false interaction. Supporting Evidence: PMID:11714716 including SmB, SmD1, SmD2, SmD3, and SmE UniProtKB:P14678 Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | REMOVE | Summary: GEMIN4 co-association is supported. Reason: Positive co-immunoprecipitation supports association within the assembly machinery. GEMIN4 complex membership alone supplies no more precise binding class or autonomous activity. Removal concerns the generic term, not the source result. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | REMOVE | Summary: The SmE interaction is retained. Reason: SmE recovery in the in-vitro assay supports this pair. An isolated Sm subunit does not by itself establish ribonucleoprotein-complex binding; no more informative partner-class term is supported. Generic protein binding is uninformative. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | REMOVE | Summary: The independently assigned SmE context is preserved. Reason: This IntAct assertion retains the same positive SmE interaction and its own original identity and date. Neither duplicate assignment nor removal of the generic term negates the pair. Sm-subunit identity alone does not establish binding to a complete RNP. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | REMOVE | Summary: The SmD1 interaction is supported. Reason: The interaction evidence is retained. SmD1 organizes an snRNP core; that does not establish the signaling-scaffold partner class described by GO:0097110. Generic protein binding adds no informative activity. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | REMOVE | Summary: The SmD2 interaction is supported. Reason: The positive SmD2 assay is retained. Its snRNP structural role does not identify a supported enzyme-, chaperone- or signaling-scaffold-binding replacement. The generic term is removed for lack of functional information. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | REMOVE | Summary: The SmD3 interaction is supported. Reason: The observed SmD3 association remains evidence for GEMIN5 interaction with assembly substrates. It does not establish binding to a complete RNP or a more precise activity of GEMIN5. Generic protein binding is uninformative. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | REMOVE | Summary: The direct SMN interaction is retained. Reason: Purified-protein binding supports the pair. The literal Q16637 record covers SMN1 and SMN2, so this row does not identify an SMN2-specific product. SMN assembly-backbone function is distinct from the signaling-scaffold definition; the generic binding term is uninformative. Supporting Evidence: PMID:11714716 Gemin5 binds SMN directly UniProtKB:Q16637 SMN1 acts as a structural backbone |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | REMOVE | Summary: The IntAct SMN context retains its independent provenance. Reason: The positive SMN interaction is retained with the original IntAct assignment and date. Q16637 does not distinguish SMN1 from SMN2 here. The generic term adds no specific function, and an assembly-backbone role alone is insufficient for the signaling-scaffold binding term. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | MODIFY | Summary: GEMIN5 associates with the DEAD-box helicase DDX20. Reason: The positive GEMIN3/DDX20 association and independently documented DEAD-box enzyme identity support a precise partner-class binding term. This does not assign helicase catalysis to GEMIN5 or claim purified binary affinity from co-immunoprecipitation. The classification is independently anchored in the Q9UHI6 SIMILARITY comment and DEAD/Helicase_C domain cross-references. Proposed replacements: DEAD/H-box RNA helicase binding Supporting Evidence: UniProtKB:Q9UHI6 Belongs to the DEAD box helicase family. DDX20 subfamily |
| GO:0005515 protein binding | IPI PMID:16739988 Quantitative proteomics identifies Gemin5, a scaffolding pro... | MODIFY | Summary: The positive eIF4E interaction supports a specific binding term. Reason: The independent recombinant-protein assay supports eIF4E binding, with the literal cytoplasmic context retained. Tagged proteins did not detectably co-immunoprecipitate in the later 293T experiment; this condition-specific negative result limits generalization but does not erase the positive direct assay. Cap binding alone is not evidence for the pair. Proposed replacements: eukaryotic initiation factor 4E binding Supporting Evidence: PMID:16739988 Gemin5 was identified as a novel eIF4E binding partner, which interacted directly with eIF4E UniProtKB:P06730 Belongs to the eukaryotic initiation factor 4E family |
| GO:0005515 protein binding | IPI PMID:17178713 A comprehensive interaction map of the human survival of mot... | REMOVE | Summary: The GEMIN2 interaction has direct source support. Reason: Selected original co-translation and recruitment experiments support this association. Assembly organization by GEMIN2 does not establish the protein-folding chaperone class. The positive pair is preserved while the uninformative generic binding annotation is removed. |
| GO:0005515 protein binding | IPI PMID:19750007 Identification of gemin5 as a novel 7-methylguanosine cap-bi... | REMOVE | Summary: Cytoplasmic GEMIN4 co-association is supported. Reason: The source supports association with GEMIN4. Neither complex membership nor colocalization establishes a more precise partner-class molecular function for this pair. Removal of the generic term does not reject that positive evidence. |
| GO:0005515 protein binding | IPI PMID:19750007 Identification of gemin5 as a novel 7-methylguanosine cap-bi... | MODIFY | Summary: The GEMIN3 association can be described by its helicase class. Reason: Positive DDX20/GEMIN3 co-association and the verified DEAD-box helicase class support the more informative binding term. The association does not establish direct purified affinity, activation of the helicase, or helicase catalysis by GEMIN5. Q9UHI6 records the DEAD-box/DDX20 family in its SIMILARITY comment, independently of the protein name. Proposed replacements: DEAD/H-box RNA helicase binding Supporting Evidence: UniProtKB:Q9UHI6 Belongs to the DEAD box helicase family. DDX20 subfamily |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: BioPlex 2 supports the SmE–GEMIN5 association. Reason: The original network contains the exact P62304–Q8TEQ6 pair. AP–MS establishes co-association, not an isolated binary affinity or a complete-RNP binding assay. SmE structural-subunit identity supplies no supported specific replacement for generic protein binding. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: BioPlex 3 independently retains the SmE association. Reason: The exact P62304–Q8TEQ6 network pair is positive. Its AP–MS evidence does not establish purified binary binding or a more precise partner-class function. Removing the generic term leaves the association and its separate source intact. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: OpenCell supports the SMN1–GEMIN5 association. Reason: The original table identifies SMN1 and GEMIN5. The literal Q16637 record includes both SMN genes, so the table is compatible at gene level without proving an SMN2-specific clone or sequence. The generic binding term is uninformative; the positive association remains. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: The U2OS interaction network supports SmE association. Reason: The retained original AP–MS network includes the SNRPE–GEMIN5 edge. This is a co-association result, without a pair-specific purified assay or isoform sequence assignment. Sm-subunit identity alone does not establish a more precise binding class. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: The inherited nuclear localization is supported in human cells. Reason: Actual PAINT descent from AN0/PTN005299808 is intact, and human nucleoplasmic/gem localization corroborates the nuclear pool. Cytoplasmic assembly activity does not exclude this independently observed location. |
| GO:0005654 nucleoplasm | IDA PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | ACCEPT | Summary: GEMIN5 has an experimentally observed nucleoplasmic pool. Reason: Human HeLa imaging distinguishes diffuse nucleoplasmic staining from concentrated gems and the cytoplasmic pool. Retain the nucleoplasmic annotation on that direct source. Supporting Evidence: |
| GO:0005654 nucleoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: The UniProt nucleoplasm mapping is supported by imaging. Reason: The curated SL-0190 localization agrees with the observed human nucleoplasmic signal. It does not assert that all GEMIN5 is nuclear or nucleolar. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-191830 | ACCEPT | Summary: GEMIN5 is represented in the nucleoplasmic import product. Reason: The official event output reaches human GEMIN5 residues 1–1508 through complex 191762 and physical entity 191765, explicitly located in the nucleoplasm. The import event itself is assigned to the nuclear envelope; that event compartment is not substituted for the target location. Supporting Evidence: Reactome:R-HSA-191830 |
| GO:0005737 cytoplasm | EXP PMID:19750007 Identification of gemin5 as a novel 7-methylguanosine cap-bi... | ACCEPT | Summary: Cap-binding GEMIN5 is recovered from human cytoplasmic preparations. Reason: The source supplies positive cytoplasmic biochemical evidence, corroborated by independent imaging. It does not establish exclusion from every organelle or from the nucleus. |
| GO:0005737 cytoplasm | EXP PMID:20513430 Gemin5 delivers snRNA precursors to the SMN complex for snRN... | ACCEPT | Summary: GEMIN5 functions in the cytoplasmic snRNA-assembly pathway. Reason: HeLa localization and captured pre-snRNA complexes support the cytoplasmic pool. Inhibitor-induced subcomplex separation is kept distinct from the untreated state. Supporting Evidence: |
| GO:0005737 cytoplasm | EXP PMID:25911097 Gemin5 Binds to the Survival Motor Neuron mRNA to Regulate S... | ACCEPT | Summary: The SMN-mRNA-binding pool is present in cytoplasmic preparations. Reason: Cytoplasmic RNA-binding and polysome experiments support this compartment. They do not establish exclusive cytoplasmic localization. Supporting Evidence: |
| GO:0005737 cytoplasm | EXP PMID:27507887 The RNA-binding protein Gemin5 binds directly to the ribosom... | ACCEPT | Summary: The ribosome-associated GEMIN5 pool is cytoplasmic. Reason: The human-cell fractionation and translation experiments support this compartment. Salt-sensitive association with ribosomal fractions is not evidence that GEMIN5 is an integral ribosomal constituent or absent from its independently demonstrated nuclear pools. Supporting Evidence: |
| GO:0005737 cytoplasm | IDA PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | ACCEPT | Summary: GEMIN5 is directly observed in the cytoplasm. Reason: HeLa microscopy provides positive cytoplasmic localization, alongside a smaller nuclear pool. The multiple locations are compatible. Supporting Evidence: |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: GEMIN5 has an established cytoplasmic pool. Reason: The SL-0086 mapping is consistent with direct localization and cytoplasmic RNA-recognition/assembly studies. This remains a useful compartment-level statement alongside more precise biochemical cytosol annotations. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: The cytosolic localization is well supported. Reason: The HPA assertion agrees with independent human cytosolic-complex and RNA-delivery experiments. This retention does not claim that the current HPA antibody images or every cellular condition were independently re-examined, nor does it exclude nuclear pools. |
| GO:0005829 cytosol | IDA PMID:18984161 An assembly chaperone collaborates with the SMN complex to g... | ACCEPT | Summary: The endogenous GEMIN5 complex is present in the cytosolic preparation. Reason: The original human HeLa cytosolic preparation includes GEMIN5 in the native SMN complex. This directly supports the compartment, without transferring the composition of the separate recombinant deletion complexes to the endogenous preparation. Supporting Evidence: |
| GO:0005829 cytosol | IDA PMID:19750007 Identification of gemin5 as a novel 7-methylguanosine cap-bi... | ACCEPT | Summary: A soluble cytosolic GEMIN5 pool supports cap recognition. Reason: Cytoplasmic lysate-based binding evidence and independent cellular localization support the curator’s cytosol claim. A complete organelle-exclusion fractionation is not attributed to this source. |
| GO:0005829 cytosol | IDA PMID:20513430 Gemin5 delivers snRNA precursors to the SMN complex for snRN... | ACCEPT | Summary: GEMIN5 participates in cytosolic pre-snRNA complex assembly. Reason: The captured complexes and cytoplasmic location support the soluble assembly compartment. Nuclear shuttling is left possible rather than excluded. Supporting Evidence: |
| GO:0005829 cytosol | TAS Reactome:R-HSA-191763 | ACCEPT | Summary: GEMIN5 occurs in the cytosolic snurportin-binding assembly intermediate. Reason: The actual input chain 191891 → 191791 → 191881 → 191833 reaches human GEMIN5 residues 1–1508 in the cytosol. This event represents snRNP–snurportin complex formation. The location is supported by the target physical entity, without assigning GEMIN5 the separate adaptor role of snurportin. Supporting Evidence: Reactome:R-HSA-191763 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-191784 | ACCEPT | Summary: The modeled GEMIN5-containing complex is cytosolic. Reason: The source input chain 191813 → 191791 → 191881 → 191833 identifies the human GEMIN5 physical entity and its cytosolic compartment. This supports location within the assembly intermediate, without converting every modeled reaction into an autonomous GEMIN5 activity. Supporting Evidence: Reactome:R-HSA-191784 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-191786 | ACCEPT | Summary: GEMIN5 is cytosolic in the modeled Sm-associated intermediate. Reason: The input complex reaches cytosolic human GEMIN5 through 191791 → 191881 → 191833. The explicit target accession and full-length residue interval support the compartment; repeated component references are not additional products. Supporting Evidence: Reactome:R-HSA-191786 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-191790 | ACCEPT | Summary: GEMIN5 belongs to the cytosolic SMN-containing input. Reason: The event input 191881 contains physical entity 191833, human GEMIN5 residues 1–1508 in the cytosol. The methylosome is recorded separately as catalyst, so this evidence supports location rather than methyltransferase activity. Supporting Evidence: Reactome:R-HSA-191790 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-191830 | ACCEPT | Summary: The nuclear-import substrate contains cytosolic GEMIN5. Reason: The import input reaches cytosolic GEMIN5 through 191778 → 191791 → 191881 → 191833. Its output separately contains nucleoplasmic GEMIN5. Both compartment assertions are compatible with the modeled import transition; the nuclear-envelope event location is not a target-localization claim. Supporting Evidence: Reactome:R-HSA-191830 |
| GO:0006417 regulation of translation | IMP PMID:25911097 Gemin5 Binds to the Survival Motor Neuron mRNA to Regulate S... | ACCEPT | Summary: GEMIN5 regulates translation of SMN mRNA. Reason: Human UTR binding and reporter, depletion and polysome experiments support a positive effect on SMN translation without a corresponding change in its mRNA abundance or stability. This transcript-specific result does not imply universal stimulation of protein synthesis. Supporting Evidence: |
| GO:0006417 regulation of translation | IMP PMID:27507887 The RNA-binding protein Gemin5 binds directly to the ribosom... | ACCEPT | Summary: GEMIN5 also modulates translation in the tested HEK293 conditions. Reason: Depletion modestly increases incorporation, while full-length or N-terminal overexpression has an opposing effect linked to ribosome association. These conditions establish translational regulation independently of the SMN-specific positive effect; they do not prove one universal direction or an elongation-stalling mechanism. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | KEEP AS NON CORE | Summary: Membrane-fraction recovery is retained as a non-core association. Reason: The incoming journal HDA assertion is preserved. Independent target rows in the author’s original thesis identify ENSP00000285873 in two TFE-resistant YTS membrane-pellet analyses, agreeing with the current GEMIN5 protein cross-reference. These corroborate fraction association, not integral insertion, a specific membrane side, direct lipid contact or quantitative enrichment. The final journal supplement was inaccessible; the thesis tables are explicitly a separate source with different study totals. The two positive identifications, including log(e) −23.2 in the RP analysis, are weighed together; fractionation alone does not establish that the recovery is an artifact. Supporting Evidence: UniProtKB:Q8TEQ6 file:human/GEMIN5/GEMIN5-deep-research-manual.md ENSP00000285873 | −23.2 | TFE-resistant YTS membrane pellet, RP analysis |
| GO:0016604 nuclear body | IDA GO_REF:0000052 | TOO GENERAL | Summary: The broad nuclear-body term is already covered by a specific location. Reason: HPA nuclear-body localization is retained as positive evidence. Independently demonstrated gems are a verified is_a descendant of nuclear body and are represented by the specific refinement of the direct-source row. The HPA foci themselves are not relabeled as gems solely from this broad assertion. TOO_GENERAL describes redundancy of the broad gene-level location, whereas MODIFY on the primary imaging row specifies what that experiment identified; these are different reasons for preferring the same child location. |
| GO:0016604 nuclear body | IDA PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | MODIFY | Summary: The observed nuclear bodies are gems. Reason: The original imaging explicitly identifies GEMIN5-positive gems with SMN colocalization. GO:0097504 is an actual is_a child of nuclear body; this specifies the observed structure without equating it with a Cajal body. The HPA assertion remains separate because its broad foci were not independently identified as gems. Proposed replacements: Gemini of Cajal bodies Supporting Evidence: PMID:11714716 where it colocalizes with SMN in gems. |
| GO:0017069 snRNA binding | IDA PMID:16857593 The Gemin5 protein of the SMN complex identifies snRNAs. | ACCEPT | Summary: GEMIN5 recognizes snRNAs during snRNP biogenesis. Reason: The original study demonstrates direct, selective snRNA recognition and impaired Sm-core assembly after depletion. This useful RNA-class function encompasses several substrates rather than one U snRNA alone. Supporting Evidence: |
| GO:0030619 U1 snRNA binding | IDA PMID:19377484 Gemin5-snRNA interaction reveals an RNA binding function for... | ACCEPT | Summary: Human GEMIN5 directly recognizes U1 snRNA. Reason: The original purified-protein experiments support U1 binding. U1 and U4 have different fragment requirements: U1 recognition extends through residues 1–844. These engineered constructs establish assay scope, not additional natural products. Supporting Evidence: |
| GO:0030619 U1 snRNA binding | IDA PMID:19750007 Identification of gemin5 as a novel 7-methylguanosine cap-bi... | ACCEPT | Summary: Human GEMIN5 associates with U1 snRNA. Reason: Cellular RNA-IP supports U1 association, with U6 as comparator. This experiment is distinct from the paper’s cap assay and is not described as purified two-component U1 affinity. Independent recognition studies corroborate the claim. |
| GO:0030619 U1 snRNA binding | IDA PMID:27881600 Structural insights into Gemin5-guided selection of pre-snRN... | ACCEPT | Summary: GEMIN5 recognizes U1 snRNA and its precursors. Reason: Human cellular pull-downs distinguish full-length pre-U1 from Sm-site-deficient truncated U1. Cap-site mutants selectively affect the latter, supporting U1 recognition without equating the two RNA forms or treating proposed P-body delivery as directly measured. Supporting Evidence: |
| GO:0030621 U4 snRNA binding | IDA PMID:19377484 Gemin5-snRNA interaction reveals an RNA binding function for... | ACCEPT | Summary: Human GEMIN5 directly binds U4 snRNA. Reason: Purified human protein and its 1–720 fragment support U4 recognition. The positive assay is retained without treating the older W286 stacking model as an experimentally solved mechanism; later structures independently refine that mechanism. |
| GO:0030621 U4 snRNA binding | IDA PMID:27881601 Structural basis for snRNA recognition by the double-WD40 re... | ACCEPT | Summary: GEMIN5 directly binds U4 snRNA. Reason: Purified human N-terminal protein binds U4 and its Sm-site fragments. Full-U4 and short-RNA mutant effects differ, so the positive interaction is retained with its RNA-construct scope rather than a universal residue-dependence claim. Supporting Evidence: |
| GO:0030622 U4atac snRNA binding | IDA PMID:20513430 Gemin5 delivers snRNA precursors to the SMN complex for snRN... | ACCEPT | Summary: GEMIN5 recognizes the U4atac precursor during snRNP assembly. Reason: The captured RNA and protected fragments establish U4atac-family recognition, particularly its precursor extension. Retain this substrate-specific claim without misdescribing the experiment as mature-U4atac affinity alone. Supporting Evidence: |
| GO:0032797 SMN complex | IBA GO_REF:0000033 | ACCEPT | Summary: GEMIN5 is an inherited SMN-complex component. Reason: Actual descent from the PAINT assertion is verified. Human complex purification independently corroborates membership; an SMN-free pool and condition-dependent dissociation do not negate the complex-associated pool. |
| GO:0032797 SMN complex | IDA PMID:17178713 A comprehensive interaction map of the human survival of mot... | ACCEPT | Summary: GEMIN5 is a component of the SMN assembly complex. Reason: The original human-cell and reconstitution experiments support peripheral incorporation of GEMIN5. Recruitment through GEMIN2 and partial dissociation under high salt are compatible with membership; they do not require permanent stoichiometry or direct binding to every subunit. Supporting Evidence: |
| GO:0032797 SMN complex | IDA PMID:18984161 An assembly chaperone collaborates with the SMN complex to g... | ACCEPT | Summary: The endogenous SMN complex contains GEMIN5. Reason: GEMIN5 is explicitly identified in the native human complex used in the original experiments. The separately constructed minimal complexes lack it by design; their activity does not contradict the composition of the endogenous complex. Supporting Evidence: |
| GO:0032797 SMN complex | IDA PMID:20513430 Gemin5 delivers snRNA precursors to the SMN complex for snRN... | ACCEPT | Summary: GEMIN5 occurs in experimentally captured SMN complexes. Reason: The source distinguishes untreated complete complexes from inhibitor-separated subcomplexes and ROS-stalled assemblies. Membership is retained without asserting that every GEMIN5 molecule always occupies the full complex. Supporting Evidence: |
| GO:0032797 SMN complex | IPI PMID:17178713 A comprehensive interaction map of the human survival of mot... | ACCEPT | Summary: The ComplexPortal SMN-complex assertion is supported. Reason: The independent IPI context retains the positive complex-assembly evidence and its original assignment. Variable incorporation efficiency does not negate membership. No autonomous enzymatic activity or universal subunit stoichiometry is inferred. Supporting Evidence: |
| GO:0034718 SMN-Gemin2 complex | IDA PMID:19377484 Gemin5-snRNA interaction reveals an RNA binding function for... | ACCEPT | Summary: GEMIN5 associates with the defined SMN–GEMIN2 core. Reason: The original Figure 5 assay detects GEMIN5 association with recombinant SMN–GEMIN2 versus the control. The GO definition requires a complex containing SMN and GEMIN2 and does not restrict it to exactly two proteins. Retain this experimentally formed association without claiming constitutive cellular stoichiometry. Supporting Evidence: |
| GO:0034719 SMN-Sm protein complex | IDA PMID:18984161 An assembly chaperone collaborates with the SMN complex to g... | ACCEPT | Summary: GEMIN5 occurs in the SMN complex associated with Sm proteins. Reason: The native complex and Sm-transfer experiments support this loaded assembly context. The definition explicitly includes Gemins 2–8 in the SMN portion. Membership does not assign GEMIN5 the autonomous catalytic activity demonstrated using other minimal components. |
| GO:0043022 ribosome binding | IDA PMID:27507887 The RNA-binding protein Gemin5 binds directly to the ribosom... | ACCEPT | Summary: GEMIN5 binds the ribosome through its N-terminal region. Reason: Purified full-length human protein binds 80S and 60S particles, with independent ribosomal-protein interactions. The experiment supports binding rather than integral ribosomal membership; the contact geometry and elongation-stalling mechanism remain models. Supporting Evidence: |
| GO:0065003 protein-containing complex assembly | TAS PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | TOO GENERAL | Summary: General complex assembly is subsumed by spliceosomal snRNP assembly. Reason: The retained GO:0000387 function is an is_a descendant of GO:0065003 through ribonucleoprotein complex assembly. It identifies the complex assembled and the work GEMIN5 performs more precisely. |
| GO:0097504 Gemini of Cajal bodies | IEA GO_REF:0000044 | ACCEPT | Summary: The gem localization mapping matches direct human observations. Reason: UniProt SL-0127 records the experimentally observed gems. Their proximity to Cajal bodies does not make the two compartments interchangeable. |
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Download this section (compressed HTML)Q: Which transcript features and cellular conditions determine whether GEMIN5 stimulates or represses translation, and how do N-terminal cap/ribosome contacts cooperate with C-terminal RNA recognition?
Q: When is GEMIN5 required for substrate selection in the cellular SMN pathway, given that simplified reconstituted complexes can assemble selected snRNP substrates without it?
Q: How stable and stoichiometric is GEMIN5 association with the SMN–GEMIN2 subcomplex in cells, compared with the positive purified-complex binding assay?
Q: What accounts for GEMIN5 recovery in the TFE-resistant NK-cell membrane fraction: a peripheral protein complex, direct lipid association, or another fractionation-dependent association?
Experiment: Compare capped snRNA and mRNA substrates using matched amounts of full-length human GEMIN5 and folding-verified site mutants. Measure RNA binding, SMN-dependent Sm loading and translation separately, keeping engineered fragments distinct from natural products.
Experiment: Use endogenous GEMIN5 perturbation with abundance-matched rescue and transcript-resolved translation measurements to distinguish direct target regulation from changes in SMN-complex abundance or global protein synthesis.
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