qkr58E-1 encodes a nuclear KH-domain RNA-binding protein associated with spliceosomal complexes. Its conserved RNA-binding architecture and recovery in Drosophila spliceosome preparations support a role in pre-mRNA processing and regulation of splicing. The native PA product is 396 residues; it regulates selected alternative-splicing events, while its exact RNA recognition sequence and any universal requirement in splicing remain unresolved.
Existing Annotations Review
GO Term
Evidence
Action
Reason
GO:0000381 regulation of alternative mRNA splicing, via spliceosome
IBA GO_REF:0000033
ACCEPT
Summary: Alternative-splicing regulation is supported by direct fly RNAi experiments and is consistent with the curated phylogenetic assignment.
Reason: PMID:27919077 Extended Data Figure 10b identifies qkr58E-1 as a regulator of fl(2)d splicing after RNAi. This directly corroborates the inherited regulation-of-splicing role without assigning universal necessity or m6A-reader activity.
IC PMID:18981222 Conservation of the protein composition and electron microsc...
ACCEPT
Summary: Retain the FlyBase assignment from affinity-purified Drosophila spliceosomal B/C complexes. The primary proteomics study supports spliceosome association and inferred participation in splicing; it does not establish catalytic activity or an absolute requirement for this protein.
Reason: Retain the FlyBase assignment from affinity-purified Drosophila spliceosomal B/C complexes. The primary proteomics study supports spliceosome association and inferred participation in splicing; it does not establish catalytic activity or an absolute requirement for this protein.
Summary: The intact KH RNA-binding domain, spliceosome association and curated phylogenetic placement support the more informative mRNA-binding assignment.
Reason: The intact KH RNA-binding domain, spliceosome association and curated phylogenetic placement support the more informative mRNA-binding assignment.
Summary: The intact KH RNA-binding domain, spliceosome association and curated phylogenetic placement support the more informative mRNA-binding assignment.
Reason: The intact KH RNA-binding domain, spliceosome association and curated phylogenetic placement support the more informative mRNA-binding assignment.
HDA PMID:25294944 Subcellular localisations of the CPTI collection of YFP-tagg...
ACCEPT
Summary: Retain the curated nuclear localization from the fly protein-trap survey, consistent with the nuclear spliceosomal role. The full study describes blinded localization followed by assignment of gene identity.
Reason: Retain the curated nuclear localization from the fly protein-trap survey, consistent with the nuclear spliceosomal role. The full study describes blinded localization followed by assignment of gene identity.
Summary: Retain the curated nuclear localization from the fly protein-trap survey, consistent with the nuclear spliceosomal role. The full study describes blinded localization followed by assignment of gene identity.
Reason: Retain the curated nuclear localization from the fly protein-trap survey, consistent with the nuclear spliceosomal role. The full study describes blinded localization followed by assignment of gene identity.
HDA PMID:18981222 Conservation of the protein composition and electron microsc...
ACCEPT
Summary: Retain the FlyBase assignment from affinity-purified Drosophila spliceosomal B/C complexes. The primary proteomics study supports spliceosome association and inferred participation in splicing; it does not establish catalytic activity or an absolute requirement for this protein.
Reason: Retain the FlyBase assignment from affinity-purified Drosophila spliceosomal B/C complexes. The primary proteomics study supports spliceosome association and inferred participation in splicing; it does not establish catalytic activity or an absolute requirement for this protein.
HDA PMID:18981222 Conservation of the protein composition and electron microsc...
ACCEPT
Summary: Retain the FlyBase assignment from affinity-purified Drosophila spliceosomal B/C complexes. The primary proteomics study supports spliceosome association and inferred participation in splicing; it does not establish catalytic activity or an absolute requirement for this protein.
Reason: Retain the FlyBase assignment from affinity-purified Drosophila spliceosomal B/C complexes. The primary proteomics study supports spliceosome association and inferred participation in splicing; it does not establish catalytic activity or an absolute requirement for this protein.
These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.
qkr58E-1 is a nuclear KH-domain RNA-binding protein associated with spliceosomes. The broad RNA-binding and gene-expression predictions are supported but less precise than existing functional assignments.
Review rationale: Spliceosomal processing and regulation of alternative mRNA splicing support a role in gene expression; existing GOA contains the more precise splicing assignments.
Supporting Evidence:
PMID:18981222: "Here we affinity purified Drosophila melanogaster spliceosomal B and C complexes formed in Kc cell nuclear extract."