EFTUD2 encodes Snu114, the GTP-binding 116-kDa subunit of the U5 small nuclear ribonucleoprotein particle. Together with PRPF8 and other U5 proteins, it organizes spliceosomal machinery used in major and minor pre-mRNA splicing. The protein is predominantly nuclear, with a smaller cytoplasmic pool associated with U5 particle assembly. Its conserved nucleotide-binding fold and RNA contacts support this ribonucleoprotein role; an active GTP-hydrolysis cycle in the human spliceosome remains unresolved. Pathogenic variants cause mandibulofacial dysostosis with microcephaly.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000244 spliceosomal tri-snRNP complex assembly | NAS PMID:38484052 Structural basis of U12-type intron engagement by the fully ... | ACCEPT | Summary: EFTUD2 contributes structural organization to the minor tri-snRNP. Reason: The human minor pre-B structure contains the U4atac/U6atac.U5 tri-snRNP, and deposited model 8Y6O explicitly contains human Q15029. EFTUD2 is a structural U5 subunit that participates in assembly of this ribonucleoprotein, rather than merely a downstream phenotype or substrate. The source is structural evidence for the assembled machinery, not an isolated EFTUD2 assembly-kinetics assay. Structural incorporation contributes to assembly of the particle; it does not by itself identify EFTUD2 as the executor of the later U11/U4atac release step assessed separately in row 3. |
| GO:0000387 spliceosomal snRNP assembly | NAS PMID:30975767 Mechanism of 5' splice site transfer for human spliceosome a... | ACCEPT | Summary: U5 subunit organization contributes to snRNP assembly. Reason: The original human HeLa tri-snRNP and pre-B structures place Snu114/EFTUD2 in the U5 structural core, with PRPF8 and Sad1-associated interfaces. Structural participation supports the existing snRNP-assembly assertion. ATP-driven remodeling attributed to PRP28 is not assigned to EFTUD2. Supporting Evidence: |
| GO:0000387 spliceosomal snRNP assembly | NAS PMID:36322420 Structural and functional investigation of the human snRNP a... | ACCEPT | Summary: The PRPF8βEFTUD2 assembly submodule supports snRNP biogenesis. Reason: The AAR2 study discusses EFTUD2 as a member of the PRPF8-containing assembly submodule. Independent human-cell experiments recover an early cytoplasmic EFTUD2 assembly pool with R2TP and PRPF8, followed by later U5 incorporation. This supports structural participation in assembly, without transferring the AAR2-specific conformational experiments or inhibitory model to EFTUD2. |
| GO:0000388 spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) | NAS PMID:38484052 Structural basis of U12-type intron engagement by the fully ... | UNDECIDED | Summary: The source-specific conformational-release role remains unresolved. Reason: The accessible abstract and deposited human minor pre-B structure establish EFTUD2 in the assembly before activation. They do not independently resolve its particular contribution to the subsequent U11/U4atac release step. The full operative article and supplement were not recovered in this audit. The positive imported NAS assertion is preserved; static membership is not treated as evidence that EFTUD2 lacks a dynamic role, nor as a direct assay of EFTUD2-powered remodeling. |
| GO:0000398 mRNA splicing, via spliceosome | IBA GO_REF:0000033 | ACCEPT | Summary: Spliceosomal pre-mRNA splicing is the conserved central process. Reason: The exact PTHR42908 path places human PTN002534021 below the spliceosome-specific PTN000562846 IBD. Literal descendant evidence includes yeast Snu114, fission-yeast Cwf10, zebrafish eftud2 and human Q15029. Human U5 binding and nuclear-extract splicing experiments, together with native spliceosome structures, corroborate the inherited role. The target appearing among donors is valid experimental descendant support, not circularity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000562846 SUPPORTS TRANSFER The literal IBD, target descent and 972-residue MSA sequence were checked. This is the spliceosomal branch, distinct from the ancestral translation-factor assertions. |
| GO:0000398 mRNA splicing, via spliceosome | IDA PMID:28076346 Cryo-EM structure of a human spliceosome activated for step ... | ACCEPT | Summary: EFTUD2 is a structural participant in spliceosomal splicing. Reason: This source describes human C* complex stalled after PRP16 action, before exon ligation; deposited 5MQF. The original deposited entity maps to human Q15029, and the existing process assertion is consistent with its structural work in the spliceosome. This does not assign RNA-cleavage catalysis or the ATPase activity of another subunit to EFTUD2. Stage-specific membership and the available article-access scope are recorded separately. Supporting Evidence: |
| GO:0000398 mRNA splicing, via spliceosome | NAS PMID:29360106 Structure of the human activated spliceosome in three confor... | ACCEPT | Summary: EFTUD2 is a structural participant in spliceosomal splicing. Reason: This source describes human activated Bact structures in early, mature and late conformations; deposited 5Z56/5Z57/5Z58. The original deposited entity maps to human Q15029, and the existing process assertion is consistent with its structural work in the spliceosome. This does not assign RNA-cleavage catalysis or the ATPase activity of another subunit to EFTUD2. Stage-specific membership and the available article-access scope are recorded separately. Supporting Evidence: |
| GO:0000398 mRNA splicing, via spliceosome | NAS PMID:30728453 Structures of the human spliceosomes before and after releas... | ACCEPT | Summary: EFTUD2 is a structural participant in spliceosomal splicing. Reason: This source describes human postcatalytic P and intron-lariat spliceosomes assembled in HeLa nuclear extract; deposited 6ICZ/6ID0/6ID1. The original deposited entity maps to human Q15029, and the existing process assertion is consistent with its structural work in the spliceosome. This does not assign RNA-cleavage catalysis or the ATPase activity of another subunit to EFTUD2. Stage-specific membership and the available article-access scope are recorded separately. Supporting Evidence: |
| GO:0000398 mRNA splicing, via spliceosome | NAS PMID:30975767 Mechanism of 5' splice site transfer for human spliceosome a... | ACCEPT | Summary: EFTUD2 is a structural participant in spliceosomal splicing. Reason: This source describes human tri-snRNP and pre-B structures purified from HeLa nuclear extract; deposited 6QW6/6QX9. The original deposited entity maps to human Q15029, and the existing process assertion is consistent with its structural work in the spliceosome. This does not assign RNA-cleavage catalysis or the ATPase activity of another subunit to EFTUD2. Stage-specific membership and the available article-access scope are recorded separately. Supporting Evidence: |
| GO:0000398 mRNA splicing, via spliceosome | NAS PMID:33509932 Structure of the activated human minor spliceosome. | ACCEPT | Summary: EFTUD2 is a structural participant in spliceosomal splicing. Reason: This source describes activated human minor spliceosome, including the U5 subunit EFTUD2; deposited 7DVQ. The original deposited entity maps to human Q15029, and the existing process assertion is consistent with its structural work in the spliceosome. This does not assign RNA-cleavage catalysis or the ATPase activity of another subunit to EFTUD2. Stage-specific membership and the available article-access scope are recorded separately. Supporting Evidence: |
| GO:0000398 mRNA splicing, via spliceosome | NAS PMID:35705093 Mechanism of exon ligation by human spliceosome. | ACCEPT | Summary: EFTUD2 is a structural participant in spliceosomal splicing. Reason: This source describes human pre-C*-I, pre-C*-II and C* intermediates after branching and before exon ligation; deposited 7W59/7W5A/7W5B. The original deposited entity maps to human Q15029, and the existing process assertion is consistent with its structural work in the spliceosome. This does not assign RNA-cleavage catalysis or the ATPase activity of another subunit to EFTUD2. Stage-specific membership and the available article-access scope are recorded separately. Supporting Evidence: |
| GO:0000398 mRNA splicing, via spliceosome | NAS PMID:38467877 Structure of the human 20S U5 snRNP. | ACCEPT | Summary: EFTUD2 is a structural participant in spliceosomal splicing. Reason: This source describes native human U5 snRNP structural organization; deposited 8Q91/8RC0. The original deposited entity maps to human Q15029, and the existing process assertion is consistent with its structural work in the spliceosome. This does not assign RNA-cleavage catalysis or the ATPase activity of another subunit to EFTUD2. Stage-specific membership and the available article-access scope are recorded separately. Supporting Evidence: |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | ACCEPT | Summary: Endogenous EFTUD2 contacts RNA in human cells. Reason: The authentic HeLa RNA-interactome workbook contains EFTUD2 at Excel row 247 of HeLa mRNA interactome.txt, with crosslinked detection, no control detection, and adjusted enrichment probabilities 0.0402986 and 0.00247737. The original method uses UV crosslinking, oligo(dT) capture and stringent denaturing washes. This supports RNA binding. The gene-level hit does not resolve a particular natural isoform or a specific EFTUD2 RNA contact site, so the broad imported term is retained. Supporting Evidence: |
| GO:0003723 RNA binding | HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ... | ACCEPT | Summary: Independent human-cell RNA capture supports RNA binding. Reason: The authentic author thesis reports EFTUD2 in the HEK293 poly(A)-RNA capture table, with a literal target row on physical page 148. Methods 3.5β3.6 describe living-cell photoreactive-nucleoside crosslinking, matched noncrosslinked SILAC controls and stringent oligo(dT) purification. This is author-deposited evidence associated with the study, not a recovered publisher supplement. It supports broad RNA binding without resolving a target transcript, contact site or natural isoform. Supporting Evidence: |
| GO:0003924 GTPase activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Conserved intrinsic GTPase capacity is retained with complex-state limits. Reason: The literal GTPase IBD lies at ancestral PTN000562745 and is inherited by the EFTUD2 branch; no same-term loss is placed on the target path. The separate translation-factor losses at PTN000562846 do not negate GTPase activity. Purified yeast Snu114 residues 72β1008 have weak measured hydrolysis, with Km 578.4 micromolar and kcat 1.012 Γ 10^-3 s^-1, suppressed by the Prp8 Snu114-binding region. Human native U5 experiments establish GTP binding, not hydrolysis. The conserved capacity is biologically defensible but is retained as non-core because an operative human hydrolysis cycle in the spliceosome is unresolved; neither zero activity nor an autonomous motor is asserted. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000562745 SUPPORTS TRANSFER Target descent and literal IBD are authentic. Weak intrinsic ortholog activity and its complex-dependent suppression are distinguished from an unmeasured human motor cycle. Supporting Evidence: GO_REF:0000033 file:human/EFTUD2/EFTUD2-source-evidence.yaml file:human/EFTUD2/EFTUD2-bioinformatics/evidence/RESULTS.md |
| GO:0003924 GTPase activity | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: The GTPase-domain mapping is plausible but does not establish an active human motor. Reason: InterPro IPR000795 matches human EFTUD2 residues 127β409 and currently maps to both GTP binding and GTPase activity. This is a genuine domain match, not a mistaken family identifier. Weak purified yeast Snu114 hydrolysis supports the ancestral capacity, while Prp8 suppresses that activity in the tested complex. Human GTP binding is directly established, but human turnover and its physiological timing remain unresolved. Retain the electronic GTPase assertion as non-core with these limits. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: InterPro:IPR000795 SUPPORTS TRANSFER The actual target domain and current GO mapping were verified; no catalytic-residue loss is inferred. Supporting Evidence: GO_REF:0000002 file:human/EFTUD2/EFTUD2-source-evidence.yaml file:human/EFTUD2/EFTUD2-bioinformatics/evidence/RESULTS.md |
| GO:0005515 protein binding | IPI PMID:16723661 The network of protein-protein interactions within the human... | MODIFY | Summary: The SNRNP200 interaction supports enzyme binding. Reason: The original human-protein two-hybrid study reports Snu114 fragments interacting with the C-terminal Brr2/SNRNP200 cassette, with independent transformants and bait controls. SNRNP200 is an ATP-dependent RNA helicase and therefore an enzyme. Its Ski2-family classification does not justify a DEAD/H-box-specific binding term. Refinement to enzyme binding identifies the verified partner class without assigning helicase activity or catalytic-site recognition to EFTUD2. Fragment interactions do not establish all natural products as equivalent. Proposed replacements: enzyme binding |
| GO:0005515 protein binding | IPI PMID:16723661 The network of protein-protein interactions within the human... | KEEP AS NON CORE | Summary: PRPF6 association is retained with the assay discrepancy explicit. Reason: The original two-hybrid experiments support human Snu114βPRPF6 association, including full-length and fragment constructs. The accompanying GST assay did not recover the pair, which the authors discuss in terms of possible affinity or tag effects. The positive assay is not erased by that negative result. PRPF6 is a spliceosomal assembly subunit; an informative, independently supported binding child was not identified, so generic binding is retained as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16723661 The network of protein-protein interactions within the human... | KEEP AS NON CORE | Summary: PRPF8 binding is a supported spliceosomal interface. Reason: The original human two-hybrid mapping supports full-length and fragment-dependent Snu114βPRPF8 interactions. PRPF8 is a central spliceosomal scaffold, but the current scaffold-protein-binding term GO:0097110 specifically defines a signaling-pathway scaffold. That definition is not established merely by PRPF8 structural organization of a spliceosome. The positive interaction remains generic non-core binding, with no requirement for an additional native-cell phenotype. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17314511 Large-scale identification of c-MYC-associated proteins usin... | MODIFY | Summary: MYC association supports DNA-binding transcription factor binding. Reason: The paper explicitly identifies U5-116kD among independently confirmed MYC-associated proteins. Literal human IntAct records include EBI-1228184/1228216 for affinity purification/co-immunoprecipitation and EBI-1228378/1228386 for cosedimentation. MYC is independently established as a DNA-binding transcription factor. The partner-class refinement does not imply EFTUD2 itself binds DNA, regulates a particular MYC promoter, or forms a purified binary complex. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: file:human/EFTUD2/EFTUD2-source-evidence.yaml file:human/EFTUD2/EFTUD2-bioinformatics/evidence/RESULTS.md |
| GO:0005515 protein binding | IPI PMID:17332742 Composition and three-dimensional EM structure of double aff... | KEEP AS NON CORE | Summary: The SF3A2-associated purification is retained with limited pair resolution. Reason: The human prespliceosome study uses anti-SF3a66/SF3A2 affinity selection. EFTUD2/U5-116K was detected only at low peptide counts in fractions 11β12, while the authors distinguish these from purer fractions 9β10 and discuss low U5/B-complex carryover. This supports the curated co-purification context, not a resolved binary SF3A2βEFTUD2 interface or stable EFTUD2 membership in the A complex. SF3A2 is a spliceosomal subunit with no informative binding-class refinement established here. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17577209 The interactome of the histone gene regulatory factor HiNF-P... | MODIFY | Summary: The curated HINFP association identifies a DNA-binding transcription factor partner. Reason: The imported IPI assertion explicitly identifies HINFP/Q9BQA5. Its independently curated function and the source abstract establish sequence-specific histone-promoter transcription-factor activity, allowing a partner-class refinement. The abstract describes a two-hybrid interaction survey, but the EFTUD2-specific table and construct boundaries were not recovered, so no pair-specific validation or downstream transcriptional effect is invented. The refinement retains the curator-supplied positive pair at its stated resolution. Proposed replacements: DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:20858735 Interactions of ErbB4 and Kap1 connect the growth factor and... | MODIFY | Summary: The ERBB4 association supports protein kinase binding. Reason: The independently recovered original reports anti-ERBB4 intracellular-domain immunoprecipitation from TPA-treated BT474 nuclear extracts with control precipitations; Table 1 identifies U5S1/U5 snRNP among the recovered proteins and reports peptide evidence; the table entry is not interpreted here as two independent experiments. U5S1_HUMAN is the verified historical Q15029 identifier. ERBB4 is a protein tyrosine kinase. This supports a protein-kinase-binding class refinement, without asserting direct contact, EFTUD2 phosphorylation, or a new signaling activity. Proposed replacements: protein kinase binding |
| GO:0005515 protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | MODIFY | Summary: The HSPB1 partner supports Hsp27 protein binding. Reason: The imported IPI pair names HSPB1/P04792, whose official record identifies Hsp27 and experimentally supported small heat-shock chaperone activity. The full original survey used human full-length proteins and fragments, nonautoactivating baits, independent transformations and repeat-positive scoring. Exact target-pair fragment boundaries were not recovered and are not inferred from other pairs. GO:0051008 precisely captures the verified partner identity without making EFTUD2 a chaperone. Proposed replacements: Hsp27 protein binding |
| GO:0005515 protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | KEEP AS NON CORE | Summary: The IK two-hybrid assertion is retained as non-core binding. Reason: The original human spliceosomal interaction survey supports the curator-supplied EFTUD2βIK/RED pair, while the exact pair-specific construct boundaries remain unverified. IK is a spliceosomal auxiliary protein; its cell-cycle and splicing roles do not by themselves establish an enzyme, DNA-binding transcription factor or cytoskeletal-protein class for this interaction. Retain the positive association without adding an autonomous EFTUD2 regulatory function. |
| GO:0005515 protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | KEEP AS NON CORE | Summary: The SF3B4 association is supported without an informative protein-binding child. Reason: The original human interaction study explicitly discusses Snu114βSF3b49 association in its fragment screen. SF3B4/Q15427 is an RNA-binding spliceosomal subunit. Binding to an RNA-binding protein is not itself RNA binding, and the exact isolated partner is not equivalent to binding a whole snRNP complex. Preserve the positive generic assertion as non-core. |
| GO:0005515 protein binding | IPI PMID:23793891 The nuclear cap-binding complex interacts with the U4/U6Β·U5 ... | MODIFY | Summary: The aggregate cap-binding-complex interaction supports complex binding. Reason: The source combines NCBP2/CBP20 and NCBP1/CBP80 in one imported assertion. Human CBP20-GFP affinity purification and reciprocal GFP-U5-116K precipitation recover the cap-binding complex. The authors explicitly could not assign all contacts to CBP20 versus CBP80, and the EFTUD2 reciprocal assay was not the RNase-resistant subset established for other U5 proteins. Protein-containing-complex binding matches this aggregate scope without manufacturing separate direct binary contacts. Proposed replacements: protein-containing complex binding |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: The PRPF6 affinity-purification association is retained. Reason: IntAct EBI-12451778 / IM-25054-139 records human PRPF6 bait and EFTUD2 prey in HEK293T tandem affinity purification with spoke expansion. The original ciliary-protein interactome includes nonciliary assemblies and applies replicate/background criteria; inclusion in that survey does not make EFTUD2 ciliary or an artifact. PRPF6 supplies no independently established informative partner class beyond the retained spliceosomal association. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | KEEP AS NON CORE | Summary: The SNRNP40 BioPlex association is retained as non-core binding. Reason: IntAct EBI-21746150 / IM-25778-2905 records human SNRNP40 bait and EFTUD2 prey by anti-tag co-immunoprecipitation in HEK293T, with spoke expansion. The BioPlex workflow uses sequence-checked ORFs and scoring that accounts for abundance and background frequency. This is a positive complex-associated pair, not a purified interface. The WD40 spliceosomal subunit class does not establish a more informative supported binding child. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30538148 Human nuclear RNAi-defective 2 (NRDE2) is an essential RNA s... | KEEP AS NON CORE | Summary: NRDE2 association is retained without inferring a new EFTUD2 function. Reason: The human-cell NRDE2-GFP study detects EFTUD2 by co-immunoprecipitation/mass spectrometry and confirms recovery by immunoblotting. NRDE2 perturbation effects are not EFTUD2 perturbation experiments, and the association does not establish a purified binary interface. The verified NRDE2 RNA-processing role supplies no specific protein-binding child established by these data, so the positive pair remains non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32703943 Mutations in FAM50A suggest that Armfield XLID syndrome is a... | KEEP AS NON CORE | Summary: Human FAM50AβEFTUD2 coassociation is retained. Reason: The source uses V5-tagged human EFTUD2 in U87 cells and anti-FAM50A co-immunoprecipitation with controls. The named ORF and reported sequence checking do not independently map every current natural product. FAM50A is an RNA-processing factor, not an established catalytic enzyme or DNA-binding transcription factor for this refinement. Retain the positive generic interaction as non-core. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: SNRNP200 association supports enzyme binding. Reason: Literal IntAct records EBI-54692312 and EBI-54928597 identify C-terminally tagged human EFTUD2 as bait in HEK293T and HCT116 anti-tag co-immunoprecipitations, with spoke expansion. These are affinity-purified complex associations, not independent binary-interface measurements. Independently verified SNRNP200 ATP-dependent helicase activity establishes the enzyme class. Refinement describes the partner, not catalytic activity of EFTUD2, a DEAD/H-box-specific interaction, or catalytic-site binding. Proposed replacements: enzyme binding |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: The PRPF6 association is retained with its source-specific scope. Reason: Literal IntAct records EBI-54692312 and EBI-54928597 identify C-terminally tagged human EFTUD2 as bait in HEK293T and HCT116 anti-tag co-immunoprecipitations, with spoke expansion. These are affinity-purified complex associations, not independent binary-interface measurements. PRPF6 is a spliceosomal assembly subunit; no informative binding child is established. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: The PRPF8 association is retained with its source-specific scope. Reason: Literal IntAct records EBI-54692312 and EBI-54928597 identify C-terminally tagged human EFTUD2 as bait in HEK293T and HCT116 anti-tag co-immunoprecipitations, with spoke expansion. These are affinity-purified complex associations, not independent binary-interface measurements. PRPF8 is a spliceosomal scaffold, whereas GO:0097110 specifically concerns signaling-pathway scaffolds; that class is not established here. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: The SNRNP40 association is retained with its source-specific scope. Reason: Literal IntAct records EBI-54692312 and EBI-54928597 identify C-terminally tagged human EFTUD2 as bait in HEK293T and HCT116 anti-tag co-immunoprecipitations, with spoke expansion. These are affinity-purified complex associations, not independent binary-interface measurements. SNRNP40 is a WD40 spliceosomal subunit; no informative binding child is established. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: SNRNP200 association supports enzyme binding. Reason: The OpenCell original uses endogenous split-fluorescent tagging in HEK293T and digitonin affinity purification with biological triplicates. The imported IPI names this positive pair; the exact target edge was not independently re-extracted from Table S4, so no uninspected confidence score or construct boundary is asserted. Independently verified SNRNP200 ATP-dependent helicase activity establishes the enzyme class. Refinement describes the partner, not catalytic activity of EFTUD2, a DEAD/H-box-specific interaction, or catalytic-site binding. Proposed replacements: enzyme binding |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: The PRPF6 association is retained with its source-specific scope. Reason: The OpenCell original uses endogenous split-fluorescent tagging in HEK293T and digitonin affinity purification with biological triplicates. The imported IPI names this positive pair; the exact target edge was not independently re-extracted from Table S4, so no uninspected confidence score or construct boundary is asserted. PRPF6 is a spliceosomal assembly subunit; no informative binding child is established. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: The SF3A2 association is retained with its source-specific scope. Reason: The OpenCell original uses endogenous split-fluorescent tagging in HEK293T and digitonin affinity purification with biological triplicates. The imported IPI names this positive pair; the exact target edge was not independently re-extracted from Table S4, so no uninspected confidence score or construct boundary is asserted. SF3A2 is a U2 snRNP protein; RNA binding by the partner does not make EFTUD2 a sequence-specific RNA-binding factor. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: The PRPF8 association is retained with its source-specific scope. Reason: The OpenCell original uses endogenous split-fluorescent tagging in HEK293T and digitonin affinity purification with biological triplicates. The imported IPI names this positive pair; the exact target edge was not independently re-extracted from Table S4, so no uninspected confidence score or construct boundary is asserted. PRPF8 is a spliceosomal scaffold, whereas GO:0097110 specifically concerns signaling-pathway scaffolds; that class is not established here. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: The SNRNP40 association is retained with its source-specific scope. Reason: The OpenCell original uses endogenous split-fluorescent tagging in HEK293T and digitonin affinity purification with biological triplicates. The imported IPI names this positive pair; the exact target edge was not independently re-extracted from Table S4, so no uninspected confidence score or construct boundary is asserted. SNRNP40 is a WD40 spliceosomal subunit; no informative binding child is established. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: The DNAJC17 association is retained with its source-specific scope. Reason: The OpenCell original uses endogenous split-fluorescent tagging in HEK293T and digitonin affinity purification with biological triplicates. The imported IPI names this positive pair; the exact target edge was not independently re-extracted from Table S4, so no uninspected confidence score or construct boundary is asserted. The DNAJC17 J-domain designation alone does not establish chaperone activity for a chaperone-binding refinement, and its reported PAX8 effects do not establish DNA-binding transcription-factor activity. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | KEEP AS NON CORE | Summary: The SNRNP200 association is retained with its source-specific scope. Reason: IntAct EBI-56902091 / IM-30059-17 identifies N-terminal BioID-tagged human EFTUD2 in K562 cells, proximity-dependent biotin identification (MI:1314), proximity type and spoke expansion. Matched no-biotin controls support a neighborhood association, which is not a physical-binding or purified-interface assay. SNRNP200 is an enzyme, but this source establishes proximity rather than physical association. Enzyme binding is supported by distinct physical-interaction sources and is not inferred solely from this neighborhood readout. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | KEEP AS NON CORE | Summary: The PRPF6 association is retained with its source-specific scope. Reason: IntAct EBI-56902091 / IM-30059-17 identifies N-terminal BioID-tagged human EFTUD2 in K562 cells, proximity-dependent biotin identification (MI:1314), proximity type and spoke expansion. Matched no-biotin controls support a neighborhood association, which is not a physical-binding or purified-interface assay. PRPF6 is a spliceosomal assembly subunit; no informative binding child is established. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | KEEP AS NON CORE | Summary: The IK association is retained with its source-specific scope. Reason: IntAct EBI-56902091 / IM-30059-17 identifies N-terminal BioID-tagged human EFTUD2 in K562 cells, proximity-dependent biotin identification (MI:1314), proximity type and spoke expansion. Matched no-biotin controls support a neighborhood association, which is not a physical-binding or purified-interface assay. IK is an auxiliary spliceosomal protein; its cell-cycle function does not establish a catalytic or cytoskeletal partner class. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | KEEP AS NON CORE | Summary: The PRPF8 association is retained with its source-specific scope. Reason: IntAct EBI-56902091 / IM-30059-17 identifies N-terminal BioID-tagged human EFTUD2 in K562 cells, proximity-dependent biotin identification (MI:1314), proximity type and spoke expansion. Matched no-biotin controls support a neighborhood association, which is not a physical-binding or purified-interface assay. PRPF8 is a spliceosomal scaffold, whereas GO:0097110 specifically concerns signaling-pathway scaffolds; that class is not established here. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: The PRPF6 association is retained with its source-specific scope. Reason: The original U2OS study uses HA/FLAG affinity-purification mass spectrometry and background-aware scoring. The imported IPI identifies this positive pair, but its exact supplemental edge and construct sequence were not independently reconstructed; no direct-contact or natural-isoform claim is added. PRPF6 is a spliceosomal assembly subunit; no informative binding child is established. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: The PRPF8 association is retained with its source-specific scope. Reason: The original U2OS study uses HA/FLAG affinity-purification mass spectrometry and background-aware scoring. The imported IPI identifies this positive pair, but its exact supplemental edge and construct sequence were not independently reconstructed; no direct-contact or natural-isoform claim is added. PRPF8 is a spliceosomal scaffold, whereas GO:0097110 specifically concerns signaling-pathway scaffolds; that class is not established here. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: The DNAJC17 association is retained with its source-specific scope. Reason: The original U2OS study uses HA/FLAG affinity-purification mass spectrometry and background-aware scoring. The imported IPI identifies this positive pair, but its exact supplemental edge and construct sequence were not independently reconstructed; no direct-contact or natural-isoform claim is added. The DNAJC17 J-domain designation alone does not establish chaperone activity for a chaperone-binding refinement, and its reported PAX8 effects do not establish DNA-binding transcription-factor activity. Preserve the positive generic assertion as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9774689 The human U5-220kD protein (hPrp8) forms a stable RNA-free c... | KEEP AS NON CORE | Summary: Direct PRPF8βEFTUD2 binding is retained. Reason: The original human U5 study isolates a stable 116/220-kDa dimer without snRNA and shows binding of labeled 116-kDa protein to PRPF8 on overlay blots. This supports the positive PRPF8 pair. The signaling-specific definition of GO:0097110 is not established by a spliceosomal scaffold, so the generic interaction remains non-core rather than being removed for lack of a more specific term. |
| GO:0005515 protein binding | IPI PMID:9774689 The human U5-220kD protein (hPrp8) forms a stable RNA-free c... | KEEP AS NON CORE | Summary: SNRNP40 association is retained at the complex level. Reason: The original human U5 fractionation and reconstitution experiments support a 40/116/220-kDa assembly. They separately show that SNRNP40 and EFTUD2 each bind PRPF8 and do not detect a direct SNRNP40βEFTUD2 interaction in the overlay assay. Thus the imported positive association is retained at complex level, not described as a demonstrated binary interface; the source does not establish an informative partner-class refinement. |
| GO:0005525 GTP binding | IEA GO_REF:0000002 | ACCEPT | Summary: GTP binding is directly established for human EFTUD2. Reason: The listed InterPro domains are authentic target matches, including the Snu114 GTP-binding domain IPR044121 at residues 130β328. Independent native human U5 experiments demonstrate specific GTP binding to the 116-kDa component. This does not establish hydrolysis from each individual domain match or an active GTP-driven translocation cycle. Propagation Review Root cause: NO FAILURE CORE Sources checked: InterPro:IPR044121 SUPPORTS TRANSFER Current target mapping and direct human nucleotide-binding evidence corroborate the combined electronic assertion. |
| GO:0005634 nucleus | EXP PMID:26912367 Molecular architecture of the human U4/U6.U5 tri-snRNP. | ACCEPT | Summary: Nuclear localization agrees with the source-specific spliceosomal pool. Reason: The source concerns 3JCR native human tri-snRNP, with a deposited EFTUD2 entity mapping to human Q15029. Nuclear spliceosomal localization is supported without treating the structural preparation as a complete cellular-distribution experiment. The broader nucleus assertion is retained at the resolution of this source; independently supported nucleoplasm and speckle pools are evaluated separately. |
| GO:0005634 nucleus | EXP PMID:28502770 An Atomic Structure of the Human Spliceosome. | ACCEPT | Summary: Nuclear localization agrees with the source-specific spliceosomal pool. Reason: The source concerns 5XJC human C*, with a deposited EFTUD2 entity mapping to human Q15029. Nuclear spliceosomal localization is supported without treating the structural preparation as a complete cellular-distribution experiment. The broader nucleus assertion is retained at the resolution of this source; independently supported nucleoplasm and speckle pools are evaluated separately. |
| GO:0005634 nucleus | EXP PMID:28781166 Cryo-EM Structure of a Pre-catalytic Human Spliceosome Prime... | ACCEPT | Summary: Nuclear localization agrees with the source-specific spliceosomal pool. Reason: The source concerns 5O9Z human B, with a deposited EFTUD2 entity mapping to human Q15029. Nuclear spliceosomal localization is supported without treating the structural preparation as a complete cellular-distribution experiment. The broader nucleus assertion is retained at the resolution of this source; independently supported nucleoplasm and speckle pools are evaluated separately. |
| GO:0005634 nucleus | EXP PMID:29301961 Structure of a human catalytic step I spliceosome. | ACCEPT | Summary: Nuclear localization agrees with the source-specific spliceosomal pool. Reason: The source concerns 5YZG human C, with a deposited EFTUD2 entity mapping to human Q15029. Nuclear spliceosomal localization is supported without treating the structural preparation as a complete cellular-distribution experiment. The broader nucleus assertion is retained at the resolution of this source; independently supported nucleoplasm and speckle pools are evaluated separately. |
| GO:0005634 nucleus | EXP PMID:29360106 Structure of the human activated spliceosome in three confor... | ACCEPT | Summary: Nuclear localization agrees with the source-specific spliceosomal pool. Reason: The source concerns 5Z56/5Z57/5Z58 human Bact, with a deposited EFTUD2 entity mapping to human Q15029. Nuclear spliceosomal localization is supported without treating the structural preparation as a complete cellular-distribution experiment. The broader nucleus assertion is retained at the resolution of this source; independently supported nucleoplasm and speckle pools are evaluated separately. |
| GO:0005634 nucleus | EXP PMID:29361316 Structure and Conformational Dynamics of the Human Spliceoso... | ACCEPT | Summary: Nuclear localization agrees with the source-specific spliceosomal pool. Reason: The source concerns 6FF4/6FF7 human Bact, with a deposited EFTUD2 entity mapping to human Q15029. Nuclear spliceosomal localization is supported without treating the structural preparation as a complete cellular-distribution experiment. The broader nucleus assertion is retained at the resolution of this source; independently supported nucleoplasm and speckle pools are evaluated separately. |
| GO:0005634 nucleus | EXP PMID:30315277 Structures of the human pre-catalytic spliceosome and its pr... | ACCEPT | Summary: Nuclear localization agrees with the source-specific spliceosomal pool. Reason: The source concerns 6AH0/6AHD human pre-B/B, with a deposited EFTUD2 entity mapping to human Q15029. Nuclear spliceosomal localization is supported without treating the structural preparation as a complete cellular-distribution experiment. The broader nucleus assertion is retained at the resolution of this source; independently supported nucleoplasm and speckle pools are evaluated separately. |
| GO:0005634 nucleus | EXP PMID:30705154 A human postcatalytic spliceosome structure reveals essentia... | ACCEPT | Summary: Nuclear localization agrees with the source-specific spliceosomal pool. Reason: The source concerns 6QDV human P, with a deposited EFTUD2 entity mapping to human Q15029. Nuclear spliceosomal localization is supported without treating the structural preparation as a complete cellular-distribution experiment. The broader nucleus assertion is retained at the resolution of this source; independently supported nucleoplasm and speckle pools are evaluated separately. |
| GO:0005634 nucleus | IDA PMID:28076346 Cryo-EM structure of a human spliceosome activated for step ... | ACCEPT | Summary: Nuclear localization agrees with the source-specific spliceosomal pool. Reason: The source concerns 5MQF human C*, with a deposited EFTUD2 entity mapping to human Q15029. Nuclear spliceosomal localization is supported without treating the structural preparation as a complete cellular-distribution experiment. The broader nucleus assertion is retained at the resolution of this source; independently supported nucleoplasm and speckle pools are evaluated separately. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: The combined nuclear-location inference is corroborated. Reason: Current ARBA00026330 has a matching Eukaryota condition set requiring IPR000640, IPR000795 and IPR031950, all present in the target. Its output is GO:0005634. UniProt subcellular-location mapping SL-0191 and independent human nuclear localization corroborate the combined IEA. This is not a conclusion drawn merely from a domain name. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00026330 SUPPORTS TRANSFER The actual rule condition set and target InterPro matches were tested; nuclear localization is independently supported. |
| GO:0005634 nucleus | NAS PMID:30975767 Mechanism of 5' splice site transfer for human spliceosome a... | ACCEPT | Summary: Nuclear localization agrees with the source-specific spliceosomal pool. Reason: The source concerns 6QW6/6QX9 human tri-snRNP/pre-B, with a deposited EFTUD2 entity mapping to human Q15029. Nuclear spliceosomal localization is supported without treating the structural preparation as a complete cellular-distribution experiment. The broader nucleus assertion is retained at the resolution of this source; independently supported nucleoplasm and speckle pools are evaluated separately. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: Supported HPA nucleoplasm localization is retained. Reason: The gene-specific HPA page assigns nucleoplasm a supported reliability level for antibody HPA022021. The same page labels cytosol and vesicles uncertain; the overall supported score must not be transferred to those separate locations. The target metadata and cell-line annotations were inspected, without a claim to have inspected the image pixels. Supporting Evidence: GO_REF:0000052 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-75079 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model Formation of AT-AC C complex has a literal participant/component path 75079 β 77470 β 77469 β 71981 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-75079 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-75081 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model Formation of AT-AC B Complex has a literal participant/component path 75081 β 77469 β 71981 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-75081 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-75082 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model ATAC spliceosome mediated Lariat formation,5' splice site cleavage has a literal participant/component path 75082 β 77473 β 71981 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-75082 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-75083 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model ATAC spliceosome mediated 3' splice site cleavage, exon ligation has a literal participant/component path 75083 β 77475 β 71981 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-75083 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770131 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model Formation of the Spliceosomal B* complex has a literal participant/component path 9770131 β 9769560 β 9769567 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-9770131 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770132 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model Formation of the Spliceosomal Pre-B complex has a literal participant/component path 9770132 β 77506 β 71981 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-9770132 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770141 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model Formation of the Spliceosomal C* complex has a literal participant/component path 9770141 β 9770138 β 9769567 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-9770141 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770142 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model Formation of the Spliceosomal B complex has a literal participant/component path 9770142 β 9769528 β 77506 β 71981 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-9770142 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770145 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model Formation of the Spliceosomal Bact complex has a literal participant/component path 9770145 β 9770126 β 71981 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-9770145 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770236 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model Formation of the Spliceosomal P complex and exon ligation has a literal participant/component path 9770236 β 9770118 β 9769567 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-9770236 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770847 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model Spliceosomal P complex dissociates yielding the intron-containing complex (ILS) and the spliced mRNP (new) has a literal participant/component path 9770847 β 9769587 β 9769567 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-9770847 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9772351 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model Disassembly of the Intron Lariat Spliceosome (new) has a literal participant/component path 9772351 β 9770234 β 9769567 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-9772351 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9794542 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model Formation of the Spliceosomal C complex containing intron lariat has a literal participant/component path 9794542 β 9794539 β 9769567 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-9794542 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9921507 | ACCEPT | Summary: The Reactome model explicitly places EFTUD2 in nucleoplasm. Reason: The current source model NS5 interacts with Spliceosome has a literal participant/component path 9921507 β 72074 β 71981 β 71883 ending at EFTUD2 entity 71883 and UniProt reference Q15029. Both the target physical entity and source event specify nucleoplasm (GO:0005654). This is an exact curated model assertion, not an independent imaging experiment or proof that EFTUD2 catalyzes the named reaction. Supporting Evidence: Reactome:R-HSA-9921507 |
| GO:0005681 spliceosomal complex | IPI PMID:30728453 Structures of the human spliceosomes before and after releas... | ACCEPT | Summary: Spliceosomal complex membership is supported. Reason: The source resolves human P and ILS complexes, 6ICZ/6ID0/6ID1; the deposited target entity explicitly maps to human Q15029. EFTUD2 is a constituent of this dynamic splicing machinery. The broad complex assertion is retained without equating all assayed stages, assigning another subunit's ATPase activity, or asserting direct contact with every copurifying component. Supporting Evidence: |
| GO:0005681 spliceosomal complex | IPI PMID:30975767 Mechanism of 5' splice site transfer for human spliceosome a... | ACCEPT | Summary: Spliceosomal complex membership is supported. Reason: The source resolves human tri-snRNP/pre-B assemblies, 6QW6/6QX9; the deposited target entity explicitly maps to human Q15029. EFTUD2 is a constituent of this dynamic splicing machinery. The broad complex assertion is retained without equating all assayed stages, assigning another subunit's ATPase activity, or asserting direct contact with every copurifying component. Supporting Evidence: |
| GO:0005681 spliceosomal complex | IPI PMID:35705093 Mechanism of exon ligation by human spliceosome. | ACCEPT | Summary: Spliceosomal complex membership is supported. Reason: The source resolves human pre-C*/C* intermediates, 7W59/7W5A/7W5B; the deposited target entity explicitly maps to human Q15029. EFTUD2 is a constituent of this dynamic splicing machinery. The broad complex assertion is retained without equating all assayed stages, assigning another subunit's ATPase activity, or asserting direct contact with every copurifying component. Supporting Evidence: |
| GO:0005681 spliceosomal complex | IPI PMID:38467877 Structure of the human 20S U5 snRNP. | ACCEPT | Summary: Spliceosomal complex membership is supported. Reason: The source resolves native human U5 snRNP, 8Q91/8RC0; the deposited target entity explicitly maps to human Q15029. EFTUD2 is a constituent of this dynamic splicing machinery. The broad complex assertion is retained without equating all assayed stages, assigning another subunit's ATPase activity, or asserting direct contact with every copurifying component. Supporting Evidence: |
| GO:0005681 spliceosomal complex | IPI PMID:39068178 Molecular basis for the activation of human spliceosome. | ACCEPT | Summary: Spliceosomal complex membership is supported. Reason: The source resolves human activated and C spliceosomes, 8I0P and 8I0Rβ8I0W; the deposited target entity explicitly maps to human Q15029. EFTUD2 is a constituent of this dynamic splicing machinery. The broad complex assertion is retained without equating all assayed stages, assigning another subunit's ATPase activity, or asserting direct contact with every copurifying component. Supporting Evidence: |
| GO:0005681 spliceosomal complex | NAS PMID:30975767 Mechanism of 5' splice site transfer for human spliceosome a... | ACCEPT | Summary: Spliceosomal complex membership is supported. Reason: The source resolves human pre-B assembly, 6QX9; the deposited target entity explicitly maps to human Q15029. EFTUD2 is a constituent of this dynamic splicing machinery. The broad complex assertion is retained without equating all assayed stages, assigning another subunit's ATPase activity, or asserting direct contact with every copurifying component. Supporting Evidence: |
| GO:0005681 spliceosomal complex | NAS PMID:38383864 Cryo-EM analyses of dimerized spliceosomes provide new insig... | ACCEPT | Summary: Spliceosomal complex membership is supported. Reason: The source resolves human B complexes, 8Q7N/8QO9; the deposited target entity explicitly maps to human Q15029. EFTUD2 is a constituent of this dynamic splicing machinery. The broad complex assertion is retained without equating all assayed stages, assigning another subunit's ATPase activity, or asserting direct contact with every copurifying component. Supporting Evidence: |
| GO:0005682 U5 snRNP | NAS PMID:36322420 Structural and functional investigation of the human snRNP a... | ACCEPT | Summary: U5 snRNP membership is supported in the assembly context. Reason: The AAR2 paper places EFTUD2 in the PRPF8-containing U5 assembly submodule and discusses its integration with U5 components. Independent human U5 purification and native structural work establish the membership. Retention of this component annotation does not transfer the AAR2-specific inhibitory model to EFTUD2. |
| GO:0005682 U5 snRNP | NAS PMID:38467877 Structure of the human 20S U5 snRNP. | ACCEPT | Summary: Native human U5 structures directly support component membership. Reason: The source resolves human U5 snRNP architecture, with the EFTUD2 entity present in deposited models 8Q91 and 8RC0. This is a complex-membership claim; protein dynamics or maturation functions ascribed experimentally to CD2BP2 are not automatically assigned to EFTUD2. Supporting Evidence: |
| GO:0005829 cytosol | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: A minor cytoplasmic assembly pool makes cytosol defensible but non-core. Reason: The cytosol IBD originates at ancestral PTN000562745 from translation-associated donors, but target ancestry alone neither proves predominant cytosolic localization nor justifies rejecting the inference. Human GFP-EFTUD2 imaging and assembly experiments independently identify a weak cytoplasmic pool and cytoplasmic R2TP-associated U5 maturation. Artificial recruitment to RPAP3-containing P-bodies is a separate assay, not evidence of normal P-body residence. HPA cytosol is uncertain. Retain cytosol as a contextual non-core pool, while nuclear splicing is dominant. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000562745 SUPPORTS TRANSFER The literal ancestral placement and EEF2/BipA donor identities were checked. Independent human assembly evidence supports a secondary cytoplasmic pool despite functional divergence from translation. |
| GO:0015030 Cajal body | IDA PMID:15257298 RNAi knockdown of hPrp31 leads to an accumulation of U4/U6 d... | KEEP AS NON CORE | Summary: The observed Cajal-body pool is retained as a secondary location. Reason: The source measures Snu114 Cajal-body/nucleoplasm ratios in HeLa cells using anti-Snu114 and coilin staining. A modest control ratio of about 1.4, with Prp31/Prp6-depletion comparisons, is not evidence of complete absence from Cajal bodies. This is a minor assembly-associated pool rather than the principal site of EFTUD2-mediated splicing, so retain it as non-core. Supporting Evidence: |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | UNDECIDED | Summary: The membrane-fraction target evidence remains unresolved. Reason: The source describes a membrane proteome from human NK-like YTS cells, including many transiently associated nonintegral proteins. The exact EFTUD2 target row, fraction and peptide evidence were not recovered; apparent XLS supplements from an earlier route are HTML challenge pages and are excluded. The annotation cannot be rejected as contamination or interpreted as integral-membrane topology from the abstract alone. Preserve the source with an unresolved verdict. Supporting Evidence: |
| GO:0016607 nuclear speck | IDA PMID:15257298 RNAi knockdown of hPrp31 leads to an accumulation of U4/U6 d... | ACCEPT | Summary: Nuclear speckle localization fits the native splicing pool. Reason: Human-cell anti-Snu114 imaging in the source establishes a predominantly nucleoplasmic/speckled distribution while examining snRNP assembly perturbations. This supports nuclear speckles as part of the normal nuclear splicing-associated pool. Prp31 and Prp6 knockdowns are not EFTUD2 perturbations, and the observation is not extended to every current natural isoform. Supporting Evidence: |
| GO:0030623 U5 snRNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: U5 snRNA contact is a conserved Snu114 binding activity. Reason: The literal U5-snRNA-binding IBD is placed at spliceosome-specific PTN000562846, with yeast Snu114 as the experimental donor. The corrected-and-republished primary abstract explicitly reports Snu114 photo-crosslinking to the 5β² side of internal loop 1 of U5 RNA in reconstituted yeast snRNPs. The exact human target descends from that node and preserves its full aligned sequence. This supports the inherited RNA contact without transferring the paper's proposed translocase mechanism as a demonstrated human activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000562846 SUPPORTS TRANSFER The literal yeast donor and source-specific RNA crosslinking evidence were verified. A single experimental descendant is adequate evidence for a considered ancestral placement. Supporting Evidence: GO_REF:0000033 file:human/EFTUD2/EFTUD2-source-evidence.yaml file:human/EFTUD2/EFTUD2-bioinformatics/evidence/RESULTS.md |
| GO:0042220 response to cocaine | IEA GO_REF:0000107 | UNDECIDED | Summary: Conservation of the rat cocaine-expression response is unresolved. Reason: The actual donor F1LM66 is rat Eftud2 and carries an RGD IEP annotation to PMID:20187946, a cocaine self-administration/abstinence transcriptomics study. This is not evidence that EFTUD2 metabolizes cocaine. The rat target probe/table and conservation of that contextual expression response in human were not independently resolved, so the electronic transfer remains undecided rather than being removed as a wrong paralog. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:F1LM66 UNRESOLVED Rat identity and current IEP donor are authentic; source-specific target measurement and transfer of the drug-response context remain unresolved. |
| GO:0046540 U4/U6 x U5 tri-snRNP complex | IBA GO_REF:0000033 | ACCEPT | Summary: Major tri-snRNP membership is conserved and directly supported. Reason: The exact PTN000562846 IBD places the major U4/U6.U5 tri-snRNP assertion on the spliceosomal branch. Human Q15029 is legitimate descendant evidence, and independent native human U5/tri-snRNP biochemistry and structures corroborate membership. The role is not inferred from the family's elongation-factor name. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000562846 SUPPORTS TRANSFER Target descent, literal IBD and human/yeast donor grounding were checked without treating a self donor as circular. |
| GO:0046540 U4/U6 x U5 tri-snRNP complex | IDA PMID:23793891 The nuclear cap-binding complex interacts with the U4/U6Β·U5 ... | ACCEPT | Summary: The cap-binding-complex study supports tri-snRNP association. Reason: The original human-cell study recovers U4/U6.U5 components in cap-binding-complex purifications and confirms reciprocal U5-116K association. This is consistent with independently established tri-snRNP membership. It does not resolve a direct interface with each CBC subunit or prove EFTUD2-specific RNase-resistant binding. |
| GO:0046540 U4/U6 x U5 tri-snRNP complex | IPI PMID:30975767 Mechanism of 5' splice site transfer for human spliceosome a... | ACCEPT | Summary: Native human tri-snRNP structure directly establishes membership. Reason: Human HeLa tri-snRNP model 6QW6 contains an explicitly mapped Q15029 entity, and the original describes its U5 core organization. The experimental assembly and sequence mapping establish membership without assigning another subunit's helicase activity to EFTUD2. Supporting Evidence: |
| GO:0048025 negative regulation of mRNA splicing, via spliceosome | NAS PMID:36322420 Structural and functional investigation of the human snRNP a... | MARK AS OVER ANNOTATED | Summary: The negative-splicing assignment exceeds the demonstrated EFTUD2-specific mechanism. Reason: The actual study tests AAR2βPRPF8 RNase-H-domain conformational compatibility and discusses EFTUD2 as an assembly-submodule member. Its splicing-inhibitory effect is itself proposed in the Discussion, rather than demonstrated as an EFTUD2 inhibitory activity. This source-specific NAS therefore overstates negative regulation by EFTUD2. The conclusion does not assert that EFTUD2 can never regulate splicing or that the paper experimentally showed an absence of regulation. Supporting Evidence: |
| GO:0071005 U2-type precatalytic spliceosome | IDA PMID:29361316 Structure and Conformational Dynamics of the Human Spliceoso... | MODIFY | Summary: The deposited activated Bact complex fits U2-type catalytic step 1 membership. Reason: GO:0071005 describes a precatalytic complex with all five snRNPs. This source instead resolves activated human Bact, blocked before branching after activation; deposited 6FF4_9 and 6FF7_9 are human Q15029 and carry the exact 972-residue canonical reference sequence. GO:0071006 explicitly includes the activated U2/U5/U6 complex after U1/U4 displacement and therefore fits the measured state. The correction is about this source's stage, not whether EFTUD2 persists in other stages. Article access is abstract plus original deposited model metadata, not a claimed full-body read. Proposed replacements: U2-type catalytic step 1 spliceosome Supporting Evidence: file:human/EFTUD2/EFTUD2-source-evidence.yaml file:human/EFTUD2/EFTUD2-bioinformatics/evidence/RESULTS.md |
| GO:0071006 U2-type catalytic step 1 spliceosome | IPI PMID:35705093 Mechanism of exon ligation by human spliceosome. | MODIFY | Summary: The pre-C*/C* structures support U2-type catalytic step 2 membership. Reason: The original abstract places pre-C*-I, pre-C*-II and C* after the branching reaction and before exon ligation. Deposited entities 7W59_2, 7W5A_3 and 7W5B_3 map exactly to human Q15029. GO:0071007 describes the complex after the first cleavage in preparation for the second step, whereas the imported GO:0071006 describes the activated first-step state. Refine this source-specific membership to the second-step term, preserving the original assertion and citation. Article access is abstract plus deposited model metadata. Proposed replacements: U2-type catalytic step 2 spliceosome Supporting Evidence: file:human/EFTUD2/EFTUD2-source-evidence.yaml file:human/EFTUD2/EFTUD2-bioinformatics/evidence/RESULTS.md |
| GO:0071006 U2-type catalytic step 1 spliceosome | IPI PMID:39068178 Molecular basis for the activation of human spliceosome. | ACCEPT | Summary: The activation-state structures support U2-type catalytic step 1 membership. Reason: The source assembles human spliceosomes in HeLa nuclear extract and resolves six activated Bact intermediates as well as C complex. The activated structures contain the U2/U5/U6 catalytic core after U4 release and include deposited human Q15029 entities. This matches the current definition of the first-step/activated spliceosome, without treating every structure in the paper as the same stage or assigning PRP2 activity to EFTUD2. Supporting Evidence: |
| GO:0071007 U2-type catalytic step 2 spliceosome | IBA GO_REF:0000033 | ACCEPT | Summary: Second-step U2 spliceosome membership is conserved. Reason: The literal PTN000562846 IBD is grounded by human Q15029 evidence and inherited by the exact target leaf. Human C* and pre-C* structures independently support the post-branching complex. A self donor is valid experimental support for the ancestral judgment, not circular evidence. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000562846 SUPPORTS TRANSFER Literal IBD, exact target descent and human C* membership were checked. |
| GO:0071007 U2-type catalytic step 2 spliceosome | IDA PMID:28076346 Cryo-EM structure of a human spliceosome activated for step ... | ACCEPT | Summary: Human C* structure supports U2-type catalytic step 2 membership. Reason: The original source describes the human complex stalled directly after PRP16 action, before exon ligation. Deposited 5MQF maps the EFTUD2 entity to human Q15029. This corresponds to the post-first-cleavage second-step compartment, not an EFTUD2-specific exon-ligation catalytic assay. Supporting Evidence: |
| GO:0071007 U2-type catalytic step 2 spliceosome | IPI PMID:35705093 Mechanism of exon ligation by human spliceosome. | ACCEPT | Summary: Human pre-C*/C* structures establish second-step membership. Reason: Deposited 7W59, 7W5A and 7W5B contain human Q15029 in complexes after branching and before exon ligation. Their stage fits GO:0071007, as distinct from the first-step term supplied by another row from this same source. The original source dictionary is preserved for both assertions. Supporting Evidence: |
| GO:0071009 U4atac/U6atac x U5 tri-snRNP complex | NAS PMID:38484052 Structural basis of U12-type intron engagement by the fully ... | ACCEPT | Summary: The human minor tri-snRNP contains EFTUD2. Reason: The source resolves the fully assembled human minor pre-B complex, including U4atac/U6atac.U5 tri-snRNP. Deposited 8Y6O maps its EFTUD2 entity to Q15029. U5 is shared with the major pathway, but that does not conflate the two distinct tri-snRNP complexes. Supporting Evidence: |
| GO:0071011 precatalytic spliceosome | IPI PMID:30975767 Mechanism of 5' splice site transfer for human spliceosome a... | ACCEPT | Summary: The native human pre-B structure supports precatalytic membership. Reason: The original HeLa pre-B assembly contains the snRNP architecture before catalytic activation, with EFTUD2 in the U5 core; deposited 6QX9 identifies human Q15029. The current general precatalytic term fits this state and does not imply that EFTUD2 is restricted to it. Supporting Evidence: |
| GO:0071011 precatalytic spliceosome | NAS PMID:38383864 Cryo-EM analyses of dimerized spliceosomes provide new insig... | ACCEPT | Summary: Human B-complex evidence supports the precatalytic compartment. Reason: The original purifies ATPΞ³S-stalled human B complexes containing uncleaved pre-mRNA and U1, U2, U4, U5 and U6 snRNAs. The molecular model explicitly includes SNU114, with deposited human Q15029 entities in 8Q7N/8QO9. The preparation supports a precatalytic state; the experimentally formed dimers are not asserted to be the endogenous supraspliceosome. Supporting Evidence: |
| GO:0071013 catalytic step 2 spliceosome | IDA PMID:11991638 Purification and characterization of native spliceosomes sui... | ACCEPT | Summary: The native C-complex preparation supports the curated second-step compartment. Reason: The source abstract describes affinity-purified native human C complexes containing splicing intermediates, after the first reaction. The imported target-specific IDA is retained in agreement with independently established EFTUD2 membership in post-branching spliceosomes. The separately indexed PMC landing page supplies only the abstract, so no uninspected peptide table or figure is claimed as independently read. |
| GO:0071014 post-mRNA release spliceosomal complex | IPI PMID:30728453 Structures of the human spliceosomes before and after releas... | ACCEPT | Summary: Human intron-lariat structures support the post-mRNA-release spliceosome. Reason: The original resolves human ILS1 and ILS2 after release of spliced mRNA, using HeLa nuclear extract and a PRP43 mutant to trap the complexes. Deposited 6ID0/6ID1 contain EFTUD2/Q15029. The mutant manipulation concerns PRP43, not an EFTUD2 ATPase assay. Supporting Evidence: |
| GO:0071016 U12-type precatalytic spliceosome | IPI PMID:38484052 Structural basis of U12-type intron engagement by the fully ... | ACCEPT | Summary: Minor pre-B architecture supports U12-type precatalytic membership. Reason: The source explicitly resolves the human minor pre-B complex with all five minor-pathway snRNAs and the shared U5 particle. Deposited 8Y6O contains Q15029. This is source-specific evidence for the preactivation minor spliceosome, separate from the activated minor Bact source. Supporting Evidence: |
| GO:0071018 U12-type catalytic step 2 spliceosome | IPI PMID:33509932 Structure of the activated human minor spliceosome. | MODIFY | Summary: The activated minor Bact structure fits U12-type catalytic step 1 membership. Reason: The source resolves activated human minor Bact, deposited as 7DVQ. Entity 7DVQ_3 explicitly maps to human Q15029 and has the exact canonical 972-residue reference sequence. GO:0071017 describes the activated U12/U5/U6atac complex after U11/U4atac displacement; GO:0071018 instead requires the post-first-cleavage second-step state. Refine to the activated first-step compartment, without claiming EFTUD2 is absent from later minor spliceosomes. The source access here is complete abstract and original deposited model metadata. Proposed replacements: U12-type catalytic step 1 spliceosome Supporting Evidence: file:human/EFTUD2/EFTUD2-source-evidence.yaml file:human/EFTUD2/EFTUD2-bioinformatics/evidence/RESULTS.md |
| GO:0071020 post-spliceosomal complex | IPI PMID:30728453 Structures of the human spliceosomes before and after releas... | ACCEPT | Summary: The postcatalytic human structures support post-spliceosomal membership. Reason: The source distinguishes the P complex containing ligated exons from subsequent ILS states after mRNA release. EFTUD2 is present in deposited human Q15029 entities across these assemblies. The broad post-spliceosomal assertion is correct and is not used to collapse the more precise post-mRNA-release claim from the same paper. Supporting Evidence: |
| GO:0071466 cellular response to xenobiotic stimulus | IEA GO_REF:0000107 | UNDECIDED | Summary: The rat xenobiotic-expression transfer remains unresolved. Reason: Current rat Eftud2/F1LM66 carries an RGD IEP annotation to the flutamide-exposure transcriptomics study PMID:24793618. The abstract specifies primary rat hepatocytes and dose-dependent expression responses, but the EFTUD2-specific table/probe and the corresponding human response were not recovered. Preserve the donor identity and imported assertion as undecided; no xenobiotic-metabolizing activity or false-paralog claim is inferred. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:F1LM66 UNRESOLVED Current rat IEP source and ortholog identity are verified; the target-specific response measurement and transfer across organism/context remain unresolved. |
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Download this section (compressed HTML)Q: Does human EFTUD2 hydrolyze GTP during a defined stage of spliceosome assembly or catalysis, and how does PRPF8 binding influence that activity?
Q: How do the three natural EFTUD2 protein products differ in U5 assembly, RNA contacts and spliceosomal function?
Q: Which EFTUD2 contacts contribute directly to activation of the minor spliceosome and release of U11 and U4atac?
Experiment: Measure nucleotide occupancy and GTP turnover of sequence-verified human EFTUD2 alone, with its PRPF8-binding region and in reconstituted U5 assemblies, using catalytic controls and parallel measurements of complex integrity.
Experiment: Map human EFTUD2 contacts to U5 RNA by targeted crosslinking in defined spliceosomal stages, distinguishing direct nucleotide contacts from copurification.
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