GEMIN5 is an RNA-binding component of the SMN machinery that selects small nuclear RNAs for spliceosomal snRNP assembly. Its tandem WD40 propellers recognize snRNA sequence elements and the RNA cap, while additional regions support oligomerization and interactions with structured mRNAs and ribosomes. It regulates translation in a transcript- and context-dependent manner and occupies predominantly cytoplasmic pools with a smaller nuclear gem-associated pool.
| 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 recognizes the methylguanosine cap of RNA. Reason: Biochemical binding and independent structural analyses establish a cap-binding site on the tandem WD40 region. This is a specific RNA-recognition activity, distinct from cap-dependent translation initiation by eIF4E. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 recognizes the Sm site and m7G cap of pre-snRNAs via two distinct binding sites |
| GO:0000340 RNA 7-methylguanosine cap binding | IDA PMID:27881600 Structural insights into Gemin5-guided selection of pre-snRN... | ACCEPT | Summary: GEMIN5 recognizes the methylguanosine cap of RNA. Reason: Biochemical binding and independent structural analyses establish a cap-binding site on the tandem WD40 region. This is a specific RNA-recognition activity, distinct from cap-dependent translation initiation by eIF4E. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 recognizes the Sm site and m7G cap of pre-snRNAs via two distinct binding sites |
| GO:0000340 RNA 7-methylguanosine cap binding | IDA PMID:27881601 Structural basis for snRNA recognition by the double-WD40 re... | ACCEPT | Summary: GEMIN5 recognizes the methylguanosine cap of RNA. Reason: Biochemical binding and independent structural analyses establish a cap-binding site on the tandem WD40 region. This is a specific RNA-recognition activity, distinct from cap-dependent translation initiation by eIF4E. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 recognizes the Sm site and m7G cap of pre-snRNAs via two distinct binding sites |
| GO:0000387 spliceosomal snRNP assembly | EXP PMID:12067652 The SMN complex, an assemblyosome of ribonucleoproteins. | ACCEPT | Summary: GEMIN5 selects snRNAs for SMN-mediated snRNP assembly. Reason: Its RNA-binding role and interactions with Sm proteins support an upstream assembly function. The annotation does not imply that GEMIN5 independently catalyzes every assembly step. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0000387 spliceosomal snRNP assembly | IBA GO_REF:0000033 | ACCEPT | Summary: GEMIN5 selects snRNAs for SMN-mediated snRNP assembly. Reason: Its RNA-binding role and interactions with Sm proteins support an upstream assembly function. The annotation does not imply that GEMIN5 independently catalyzes every assembly step. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0000387 spliceosomal snRNP assembly | IDA PMID:18984161 An assembly chaperone collaborates with the SMN complex to g... | ACCEPT | Summary: GEMIN5 selects snRNAs for SMN-mediated snRNP assembly. Reason: Its RNA-binding role and interactions with Sm proteins support an upstream assembly function. The annotation does not imply that GEMIN5 independently catalyzes every assembly step. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0000387 spliceosomal snRNP assembly | TAS PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | ACCEPT | Summary: GEMIN5 selects snRNAs for SMN-mediated snRNP assembly. Reason: Its RNA-binding role and interactions with Sm proteins support an upstream assembly function. The annotation does not imply that GEMIN5 independently catalyzes every assembly step. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0000398 mRNA splicing, via spliceosome | TAS PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: snRNP biogenesis supplies the splicing machinery. Reason: GEMIN5 participates in pre-mRNA splicing through production of spliceosomal snRNPs. Retain this broader process without assigning spliceosomal catalytic activity. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | ACCEPT | Summary: GEMIN5 is an experimentally established RNA-binding protein. Reason: Specific snRNA and mRNA interactions establish the broad RNA-binding function independently of the high-throughput capture row. More specific RNA-substrate activities are represented in the other annotations. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. |
| GO:0003723 RNA binding | IPI PMID:34424823 The RBS1 domain of Gemin5 is intrinsically unstructured and ... | ACCEPT | Summary: GEMIN5 is an experimentally established RNA-binding protein. Reason: Specific snRNA and mRNA interactions establish the broad RNA-binding function independently of the high-throughput capture row. More specific RNA-substrate activities are represented in the other annotations. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. |
| GO:0003730 mRNA 3'-UTR binding | IBA GO_REF:0000033 | ACCEPT | Summary: GEMIN5 binds the SMN mRNA 3′-UTR. Reason: The primary study establishes direct, sequence/structure-dependent binding. This evidence supports the function independently of the ARBA row; ARBA agreement supplies no additional validation. Supporting Evidence: PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. |
| GO:0003730 mRNA 3'-UTR binding | IDA PMID:25911097 Gemin5 Binds to the Survival Motor Neuron mRNA to Regulate S... | ACCEPT | Summary: GEMIN5 binds the SMN mRNA 3′-UTR. Reason: The primary study establishes direct, sequence/structure-dependent binding. This evidence supports the function independently of the ARBA row; ARBA agreement supplies no additional validation. Supporting Evidence: PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. |
| GO:0003730 mRNA 3'-UTR binding | IEA GO_REF:0000117 | ACCEPT | Summary: GEMIN5 binds the SMN mRNA 3′-UTR. Reason: The primary study establishes direct, sequence/structure-dependent binding. This evidence supports the function independently of the ARBA row; ARBA agreement supplies no additional validation. Supporting Evidence: PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: The recorded interactions reflect SMN-complex assembly. Reason: The original identification and interaction-map studies place GEMIN5 with SMN and Sm proteins. Retain the physical-interaction records while describing the core activity through specific RNA recognition and assembly, rather than generic protein binding. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: The recorded interactions reflect SMN-complex assembly. Reason: The original identification and interaction-map studies place GEMIN5 with SMN and Sm proteins. Retain the physical-interaction records while describing the core activity through specific RNA recognition and assembly, rather than generic protein binding. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: The recorded interactions reflect SMN-complex assembly. Reason: The original identification and interaction-map studies place GEMIN5 with SMN and Sm proteins. Retain the physical-interaction records while describing the core activity through specific RNA recognition and assembly, rather than generic protein binding. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: The recorded interactions reflect SMN-complex assembly. Reason: The original identification and interaction-map studies place GEMIN5 with SMN and Sm proteins. Retain the physical-interaction records while describing the core activity through specific RNA recognition and assembly, rather than generic protein binding. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: The recorded interactions reflect SMN-complex assembly. Reason: The original identification and interaction-map studies place GEMIN5 with SMN and Sm proteins. Retain the physical-interaction records while describing the core activity through specific RNA recognition and assembly, rather than generic protein binding. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: The recorded interactions reflect SMN-complex assembly. Reason: The original identification and interaction-map studies place GEMIN5 with SMN and Sm proteins. Retain the physical-interaction records while describing the core activity through specific RNA recognition and assembly, rather than generic protein binding. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: The recorded interactions reflect SMN-complex assembly. Reason: The original identification and interaction-map studies place GEMIN5 with SMN and Sm proteins. Retain the physical-interaction records while describing the core activity through specific RNA recognition and assembly, rather than generic protein binding. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: The recorded interactions reflect SMN-complex assembly. Reason: The original identification and interaction-map studies place GEMIN5 with SMN and Sm proteins. Retain the physical-interaction records while describing the core activity through specific RNA recognition and assembly, rather than generic protein binding. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0005515 protein binding | IPI PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: The recorded interactions reflect SMN-complex assembly. Reason: The original identification and interaction-map studies place GEMIN5 with SMN and Sm proteins. Retain the physical-interaction records while describing the core activity through specific RNA recognition and assembly, rather than generic protein binding. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0005515 protein binding | IPI PMID:16739988 Quantitative proteomics identifies Gemin5, a scaffolding pro... | KEEP AS NON CORE | Summary: GEMIN5 associates with cap-related translation machinery. Reason: The eIF4E interaction is characterized in quantitative proteomics and the cap-binding study. It is compatible with RNA-complex recruitment, but generic binding is not a distinct core activity. Supporting Evidence: PMID:16739988 The WD-repeat, scaffolding-protein Gemin5 was identified as a novel eIF4E binding partner |
| GO:0005515 protein binding | IPI PMID:17178713 A comprehensive interaction map of the human survival of mot... | KEEP AS NON CORE | Summary: The recorded interactions reflect SMN-complex assembly. Reason: The original identification and interaction-map studies place GEMIN5 with SMN and Sm proteins. Retain the physical-interaction records while describing the core activity through specific RNA recognition and assembly, rather than generic protein binding. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0005515 protein binding | IPI PMID:19750007 Identification of gemin5 as a novel 7-methylguanosine cap-bi... | KEEP AS NON CORE | Summary: GEMIN5 associates with cap-related translation machinery. Reason: The eIF4E interaction is characterized in quantitative proteomics and the cap-binding study. It is compatible with RNA-complex recruitment, but generic binding is not a distinct core activity. Supporting Evidence: PMID:16739988 The WD-repeat, scaffolding-protein Gemin5 was identified as a novel eIF4E binding partner |
| GO:0005515 protein binding | IPI PMID:19750007 Identification of gemin5 as a novel 7-methylguanosine cap-bi... | KEEP AS NON CORE | Summary: GEMIN5 associates with cap-related translation machinery. Reason: The eIF4E interaction is characterized in quantitative proteomics and the cap-binding study. It is compatible with RNA-complex recruitment, but generic binding is not a distinct core activity. Supporting Evidence: PMID:16739988 The WD-repeat, scaffolding-protein Gemin5 was identified as a novel eIF4E binding partner |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | UNDECIDED | Summary: The exact high-throughput interaction requires its gene-specific assay record. Reason: The cached study text describes a large interaction or cell-mapping dataset but does not expose the GEMIN5-specific partner evidence needed to verify this row. This is an evidence-access limitation, not grounds to remove a curated experimental interaction. Check the supporting supplementary interaction record. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | UNDECIDED | Summary: The exact high-throughput interaction requires its gene-specific assay record. Reason: The cached study text describes a large interaction or cell-mapping dataset but does not expose the GEMIN5-specific partner evidence needed to verify this row. This is an evidence-access limitation, not grounds to remove a curated experimental interaction. Check the supporting supplementary interaction record. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | UNDECIDED | Summary: The exact high-throughput interaction requires its gene-specific assay record. Reason: The cached study text describes a large interaction or cell-mapping dataset but does not expose the GEMIN5-specific partner evidence needed to verify this row. This is an evidence-access limitation, not grounds to remove a curated experimental interaction. Check the supporting supplementary interaction record. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | UNDECIDED | Summary: The exact high-throughput interaction requires its gene-specific assay record. Reason: The cached study text describes a large interaction or cell-mapping dataset but does not expose the GEMIN5-specific partner evidence needed to verify this row. This is an evidence-access limitation, not grounds to remove a curated experimental interaction. Check the supporting supplementary interaction record. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: GEMIN5 has a nuclear gem-associated pool. Reason: Immunolocalization detects GEMIN5 in nuclei and gems, although much of its characterized RNA-assembly and translation work occurs in the cytoplasm. Retain the nuclear location as a real additional pool. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. |
| GO:0005654 nucleoplasm | IDA PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: GEMIN5 has a nuclear gem-associated pool. Reason: Immunolocalization detects GEMIN5 in nuclei and gems, although much of its characterized RNA-assembly and translation work occurs in the cytoplasm. Retain the nuclear location as a real additional pool. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. |
| GO:0005654 nucleoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: GEMIN5 has a nuclear gem-associated pool. Reason: Immunolocalization detects GEMIN5 in nuclei and gems, although much of its characterized RNA-assembly and translation work occurs in the cytoplasm. Retain the nuclear location as a real additional pool. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-191830 | KEEP AS NON CORE | Summary: GEMIN5 has a nuclear gem-associated pool. Reason: Immunolocalization detects GEMIN5 in nuclei and gems, although much of its characterized RNA-assembly and translation work occurs in the cytoplasm. Retain the nuclear location as a real additional pool. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. |
| GO:0005737 cytoplasm | EXP PMID:19750007 Identification of gemin5 as a novel 7-methylguanosine cap-bi... | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005737 cytoplasm | EXP PMID:20513430 Gemin5 delivers snRNA precursors to the SMN complex for snRN... | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005737 cytoplasm | EXP PMID:25911097 Gemin5 Binds to the Survival Motor Neuron mRNA to Regulate S... | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005737 cytoplasm | EXP PMID:27507887 The RNA-binding protein Gemin5 binds directly to the ribosom... | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005737 cytoplasm | IDA PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005829 cytosol | IDA PMID:18984161 An assembly chaperone collaborates with the SMN complex to g... | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005829 cytosol | IDA PMID:19750007 Identification of gemin5 as a novel 7-methylguanosine cap-bi... | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005829 cytosol | IDA PMID:20513430 Gemin5 delivers snRNA precursors to the SMN complex for snRN... | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-191763 | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-191784 | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-191786 | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-191790 | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-191830 | ACCEPT | Summary: GEMIN5 acts in cytoplasmic RNA complexes. Reason: The original localization and subsequent snRNP/translation studies support cytoplasmic and cytosolic localization. These compartment assignments agree with substrate recognition before nuclear snRNP import. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. PMID:25911097 Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0006417 regulation of translation | IMP PMID:25911097 Gemin5 Binds to the Survival Motor Neuron mRNA to Regulate S... | ACCEPT | Summary: GEMIN5 regulates translation through RNA and ribosome interactions. Reason: Direct SMN-UTR binding promotes SMN translation, while ribosome-associated GEMIN5 can have other regulatory effects. The broad regulatory term appropriately accommodates transcript-dependent directionality. Supporting Evidence: PMID:25911097 Gemin5 binding to the SMN 3′-UTR activates expression of SMN protein by increasing translation of the SMN mRNA. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0006417 regulation of translation | IMP PMID:27507887 The RNA-binding protein Gemin5 binds directly to the ribosom... | ACCEPT | Summary: GEMIN5 regulates translation through RNA and ribosome interactions. Reason: Direct SMN-UTR binding promotes SMN translation, while ribosome-associated GEMIN5 can have other regulatory effects. The broad regulatory term appropriately accommodates transcript-dependent directionality. Supporting Evidence: PMID:25911097 Gemin5 binding to the SMN 3′-UTR activates expression of SMN protein by increasing translation of the SMN mRNA. PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | UNDECIDED | Summary: The high-throughput membrane association needs assay-specific confirmation. Reason: The principal characterized pools are cytoplasmic and nuclear. These do not exclude membrane association, but the cached evidence does not establish whether GEMIN5 was an authentic membrane-associated species in this proteomic fraction. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. |
| GO:0016604 nuclear body | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: GEMIN5 has a nuclear gem-associated pool. Reason: Immunolocalization detects GEMIN5 in nuclei and gems, although much of its characterized RNA-assembly and translation work occurs in the cytoplasm. Retain the nuclear location as a real additional pool. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. |
| GO:0016604 nuclear body | IDA PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: GEMIN5 has a nuclear gem-associated pool. Reason: Immunolocalization detects GEMIN5 in nuclei and gems, although much of its characterized RNA-assembly and translation work occurs in the cytoplasm. Retain the nuclear location as a real additional pool. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, 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 directly recognizes Sm-class snRNAs. Reason: Sequence recognition and RNA-bound structures support binding to the recorded snRNA substrates. The specific U1/U4/U4atac annotations describe substrate recognition in assembly, not catalytic RNA processing. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs |
| GO:0030619 U1 snRNA binding | IDA PMID:19377484 Gemin5-snRNA interaction reveals an RNA binding function for... | ACCEPT | Summary: GEMIN5 directly recognizes Sm-class snRNAs. Reason: Sequence recognition and RNA-bound structures support binding to the recorded snRNA substrates. The specific U1/U4/U4atac annotations describe substrate recognition in assembly, not catalytic RNA processing. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs |
| GO:0030619 U1 snRNA binding | IDA PMID:19750007 Identification of gemin5 as a novel 7-methylguanosine cap-bi... | ACCEPT | Summary: GEMIN5 directly recognizes Sm-class snRNAs. Reason: Sequence recognition and RNA-bound structures support binding to the recorded snRNA substrates. The specific U1/U4/U4atac annotations describe substrate recognition in assembly, not catalytic RNA processing. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs |
| GO:0030619 U1 snRNA binding | IDA PMID:27881600 Structural insights into Gemin5-guided selection of pre-snRN... | ACCEPT | Summary: GEMIN5 directly recognizes Sm-class snRNAs. Reason: Sequence recognition and RNA-bound structures support binding to the recorded snRNA substrates. The specific U1/U4/U4atac annotations describe substrate recognition in assembly, not catalytic RNA processing. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs |
| GO:0030621 U4 snRNA binding | IDA PMID:19377484 Gemin5-snRNA interaction reveals an RNA binding function for... | ACCEPT | Summary: GEMIN5 directly recognizes Sm-class snRNAs. Reason: Sequence recognition and RNA-bound structures support binding to the recorded snRNA substrates. The specific U1/U4/U4atac annotations describe substrate recognition in assembly, not catalytic RNA processing. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs |
| GO:0030621 U4 snRNA binding | IDA PMID:27881601 Structural basis for snRNA recognition by the double-WD40 re... | ACCEPT | Summary: GEMIN5 directly recognizes Sm-class snRNAs. Reason: Sequence recognition and RNA-bound structures support binding to the recorded snRNA substrates. The specific U1/U4/U4atac annotations describe substrate recognition in assembly, not catalytic RNA processing. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs |
| GO:0030622 U4atac snRNA binding | IDA PMID:20513430 Gemin5 delivers snRNA precursors to the SMN complex for snRN... | ACCEPT | Summary: GEMIN5 directly recognizes Sm-class snRNAs. Reason: Sequence recognition and RNA-bound structures support binding to the recorded snRNA substrates. The specific U1/U4/U4atac annotations describe substrate recognition in assembly, not catalytic RNA processing. Supporting Evidence: PMID:27881600 the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs |
| GO:0032797 SMN complex | IBA GO_REF:0000033 | ACCEPT | Summary: GEMIN5 participates in the SMN snRNP-assembly machinery. Reason: The original interaction and assembly studies establish membership and contacts with SMN/Sm components. These complex annotations describe assembly intermediates and machinery membership, not an independently catalytic GEMIN5 activity. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0032797 SMN complex | IDA PMID:17178713 A comprehensive interaction map of the human survival of mot... | ACCEPT | Summary: GEMIN5 participates in the SMN snRNP-assembly machinery. Reason: The original interaction and assembly studies establish membership and contacts with SMN/Sm components. These complex annotations describe assembly intermediates and machinery membership, not an independently catalytic GEMIN5 activity. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0032797 SMN complex | IDA PMID:18984161 An assembly chaperone collaborates with the SMN complex to g... | ACCEPT | Summary: GEMIN5 participates in the SMN snRNP-assembly machinery. Reason: The original interaction and assembly studies establish membership and contacts with SMN/Sm components. These complex annotations describe assembly intermediates and machinery membership, not an independently catalytic GEMIN5 activity. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0032797 SMN complex | IDA PMID:20513430 Gemin5 delivers snRNA precursors to the SMN complex for snRN... | ACCEPT | Summary: GEMIN5 participates in the SMN snRNP-assembly machinery. Reason: The original interaction and assembly studies establish membership and contacts with SMN/Sm components. These complex annotations describe assembly intermediates and machinery membership, not an independently catalytic GEMIN5 activity. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0032797 SMN complex | IPI PMID:17178713 A comprehensive interaction map of the human survival of mot... | ACCEPT | Summary: GEMIN5 participates in the SMN snRNP-assembly machinery. Reason: The original interaction and assembly studies establish membership and contacts with SMN/Sm components. These complex annotations describe assembly intermediates and machinery membership, not an independently catalytic GEMIN5 activity. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0034718 SMN-Gemin2 complex | IDA PMID:19377484 Gemin5-snRNA interaction reveals an RNA binding function for... | ACCEPT | Summary: GEMIN5 participates in the SMN snRNP-assembly machinery. Reason: The original interaction and assembly studies establish membership and contacts with SMN/Sm components. These complex annotations describe assembly intermediates and machinery membership, not an independently catalytic GEMIN5 activity. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0034719 SMN-Sm protein complex | IDA PMID:18984161 An assembly chaperone collaborates with the SMN complex to g... | ACCEPT | Summary: GEMIN5 participates in the SMN snRNP-assembly machinery. Reason: The original interaction and assembly studies establish membership and contacts with SMN/Sm components. These complex annotations describe assembly intermediates and machinery membership, not an independently catalytic GEMIN5 activity. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0043022 ribosome binding | IDA PMID:27507887 The RNA-binding protein Gemin5 binds directly to the ribosom... | ACCEPT | Summary: GEMIN5 binds ribosome particles through its N-terminal region. Reason: The primary biochemical fractionation and binding experiments establish this interaction as part of translation regulation. Supporting Evidence: PMID:27507887 His-Gemin5 binds to ribosome particles via its N-terminal domain. |
| GO:0065003 protein-containing complex assembly | TAS PMID:11714716 Gemin5, a novel WD repeat protein component of the SMN compl... | KEEP AS NON CORE | Summary: GEMIN5 contributes to ribonucleoprotein complex assembly. Reason: The broad protein-complex-assembly term is consistent with SMN/Sm interactions, although spliceosomal snRNP assembly is the more informative process. Supporting Evidence: PMID:11714716 Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly. |
| GO:0097504 Gemini of Cajal bodies | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: GEMIN5 has a nuclear gem-associated pool. Reason: Immunolocalization detects GEMIN5 in nuclei and gems, although much of its characterized RNA-assembly and translation work occurs in the cytoplasm. Retain the nuclear location as a real additional pool. Supporting Evidence: PMID:11714716 Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and in the nucleus, where it colocalizes with SMN in gems. |
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