id: A0A9L0R5P7 gene_symbol: GEMIN5 taxon: id: NCBITaxon:9796 label: Equus caballus status: COMPLETE description: The nuclear prediction is broad but supported. Four RNA-function predictions are uncertain for a horse model with a WD40-boundary deletion; protein-ubiquitination participation lacks a demonstrated mechanism. source_documents: - projects/PROTNLM_EVALUATION/mammal-benchmark/horse40-predictions.csv - projects/PROTNLM_EVALUATION/mammal-benchmark/predictions.jsonl.gz - projects/PROTNLM_EVALUATION/mammal-benchmark/paired-sequences/GEMIN5.json references: - id: PMID:27881600 title: Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly. full_text_unavailable: true findings: [] - id: PMID:11714716 title: Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins. full_text_unavailable: true findings: [] - id: file:HORSE/GEMIN5/GEMIN5-uniprot.txt title: HORSE/GEMIN5/GEMIN5-uniprot.txt findings: [] - id: file:HORSE/GEMIN5/GEMIN5-bioinformatics/RESULTS.md title: HORSE/GEMIN5/GEMIN5-bioinformatics/RESULTS.md findings: [] - id: PMID:25911097 title: Gemin5 Binds to the Survival Motor Neuron mRNA to Regulate SMN Expression. full_text_unavailable: false findings: [] - id: PMID:27507887 title: The RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translation. full_text_unavailable: false findings: [] predictions: - source_method: ProtNLM2 source_version: UniProt API snapshot 2026-09-08 predicted_term: id: GO:0000387 label: spliceosomal snRNP assembly predicted_term_type: GO_BP review: assessment: UNC confidence_score: 1 summary: Human GEMIN5 studies establish snRNP assembly. The selected horse protein is a close GEMIN5 relative but lacks aligned human residues723–798, spanning the end of the tandem-WD40 RNA-recognition module and adjacent sequence. The intact gene-family role is supported; the deletion makes transfer of this specific functional claim to the selected model uncertain. The conserved C-terminal regions do not independently demonstrate that its RNA-recognition and assembly machinery remains functional. supported_by: - &id001 reference_id: PMID:27881600 supporting_text: 'the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs' - reference_id: PMID:11714716 supporting_text: "Gemin5 interacts with several of the \nsnRNP core proteins including SmB, SmD1,\ \ SmD2, SmD3, and SmE, suggesting that it \nparticipates in the activities of the SMN complex\ \ in snRNP assembly." - &id002 reference_id: file:HORSE/GEMIN5/GEMIN5-uniprot.txt supporting_text: DR InterPro; IPR052640; Gemin-5. - &id003 reference_id: file:HORSE/GEMIN5/GEMIN5-bioinformatics/RESULTS.md supporting_text: share 89.2% identity among - &id004 reference_id: file:HORSE/GEMIN5/GEMIN5-bioinformatics/RESULTS.md supporting_text: The horse sequence lacks the aligned human segment 723–798. - source_method: ProtNLM2 source_version: UniProt API snapshot 2026-09-08 predicted_term: id: GO:0016567 label: protein ubiquitination predicted_term_type: GO_BP review: assessment: UNC confidence_score: 1 summary: The retrieved primary studies establish GEMIN5 RNA recognition, snRNP assembly and translation regulation. They do not establish a role executing or regulating protein ubiquitination. Being ubiquitinated, interacting with a ubiquitin-system protein, or changing proteostasis indirectly is insufficient for this process assignment. A direct mechanistic contribution to the ubiquitination process is needed; the absence of a catalytic ubiquitin-ligase domain alone would not refute noncatalytic participation. supported_by: - *id001 - &id005 reference_id: PMID:25911097 supporting_text: Gemin5 binding to the SMN 3′-UTR activates expression of SMN protein by increasing translation of the SMN mRNA. - *id002 - source_method: ProtNLM2 source_version: UniProt API snapshot 2026-09-08 predicted_term: id: GO:0005634 label: nucleus predicted_term_type: GO_CC review: assessment: LSP confidence_score: 2 summary: Human imaging establishes a nuclear GEMIN5 pool, consistent with the conserved horse protein architecture. The frozen horse GOA already has the more specific nucleoplasm location, whose biological rationale is supported by the human imaging. The predicted nucleus term is therefore less specific; it does not imply GEMIN5 is primarily nuclear or prove that its altered RNA-binding module is functional. supported_by: - reference_id: PMID:11714716 supporting_text: "Immunolocalization studies demonstrate that Gemin5 is found in the cytoplasm and\ \ \nin the nucleus, where it colocalizes with SMN in gems." - *id002 - *id003 - source_method: ProtNLM2 source_version: UniProt API snapshot 2026-09-08 predicted_term: id: GO:0000340 label: RNA 7-methylguanosine cap binding predicted_term_type: GO_MF review: assessment: UNC confidence_score: 1 summary: Human GEMIN5 studies establish RNA cap binding. The selected horse protein is a close GEMIN5 relative but lacks aligned human residues723–798, spanning the end of the tandem-WD40 RNA-recognition module and adjacent sequence. The intact gene-family role is supported; the deletion makes transfer of this specific functional claim to the selected model uncertain. The conserved C-terminal regions do not independently demonstrate that its RNA-recognition and assembly machinery remains functional. supported_by: - reference_id: PMID:27881600 supporting_text: 'the WD40 domain of Gemin5 recognizes the Sm site and m7G cap of pre-snRNAs via two distinct binding sites' - *id002 - *id003 - *id004 - source_method: ProtNLM2 source_version: UniProt API snapshot 2026-09-08 predicted_term: id: GO:0003730 label: mRNA 3'-UTR binding predicted_term_type: GO_MF review: assessment: UNC confidence_score: 1 summary: Human GEMIN5 studies establish SMN mRNA 3′-UTR binding. The selected horse protein is a close GEMIN5 relative but lacks aligned human residues723–798, spanning the end of the tandem-WD40 RNA-recognition module and adjacent sequence. The intact gene-family role is supported; the deletion makes transfer of this specific functional claim to the selected model uncertain. The conserved C-terminal regions do not independently demonstrate that its RNA-recognition and assembly machinery remains functional. supported_by: - reference_id: PMID:25911097 supporting_text: Gemin5 directly binds to the mature SMN 3′-UTR immediately upstream of the poly(A) tail. - *id002 - *id003 - *id004 - source_method: ProtNLM2 source_version: UniProt API snapshot 2026-09-08 predicted_term: id: GO:0006417 label: regulation of translation predicted_term_type: GO_BP review: assessment: UNC confidence_score: 1 summary: Human GEMIN5 studies establish translation regulation. The selected horse protein is a close GEMIN5 relative but lacks aligned human residues723–798, spanning the end of the tandem-WD40 RNA-recognition module and adjacent sequence. The intact gene-family role is supported; the deletion makes transfer of this specific functional claim to the selected model uncertain. The conserved C-terminal regions do not independently demonstrate that its RNA-recognition and assembly machinery remains functional. supported_by: - *id005 - reference_id: PMID:27507887 supporting_text: 'His-Gemin5 binds to ribosome particles via its N-terminal domain.' - *id002 - *id003 - *id004