The route by which AGGF1 acquired GO:0003676 nucleic acid binding, from InterPro:IPR000467 G-patch domain. Across the eleven reviewed human G-patch proteins QuickGO returns in full, this mapping is the sole source of the term in every case and is never corroborated experimentally in any of them.

Source of both IBA rows. One is self-referential (GO:0005576, WITH/FROM UniProtKB:Q8N302) and one draws on the zebrafish orthologue aggf1, which carries its own IMP for the propagated term. Both propagations check out.

Source of the GO:0005576 and GO:0005737 IEA rows, both faithful transfers of UniProt locations that are themselves ECO:0000269-tagged to PMID:14961121.

Purified recombinant AGGF1 promotes angiogenesis in the chick chorioallantoic membrane assay as potently as VEGF, and two siRNAs plus an antisense oligonucleotide inhibit endothelial tube formation.

AGGF1 is secreted by endothelial cells when tube formation begins, detected by competitive ELISA on conditioned medium and by metabolic labelling.

AGGF1 interacts with TNFSF12/TWEAK, shown by yeast two-hybrid, GST pull-down with recombinant proteins, and co-immunoprecipitation from cells.

The E133K association with Klippel-Trenaunay syndrome, which this paper reports, has since been refuted (see PMID:16443853, PMID:18564129). The biochemical results on the wild-type protein are unaffected.

A review by the authors of PMID:14961121 restating that paper's angiogenesis result. It contains no vasculogenesis experiment, although it is the cited source of AGGF1's GO:0001570 TAS row.

CCSB-HI1 yeast two-hybrid screen; source of the AGGF1-BLOC1S6 row. The partner is corroborated by an orthogonal co-immunoprecipitation in PMID:33961781.

An all-versus-all two-hybrid matrix of proteins that copurify with human spliceosomes. AGGF1's inclusion in that bait set is independent evidence, from a laboratory with no stake in AGGF1's vascular biology, that the protein is spliceosome-associated.

HI-II-14 two-hybrid map; the second independent source of the AGGF1 self-interaction row.

Variant-interactome two-hybrid study; one of three sources of the AGGF1-MAB21L3 row.

The HuRI reference interactome, and the source of four AGGF1 interaction rows at once - DHX15, MCRS1, FBXO28 and MAB21L3. Three of the four partners - DHX15, MCRS1 and FBXO28 - carry GO:0005634 nucleus with experimental evidence; MAB21L3 has no cellular-component annotation at all. Each pair is logged in IntAct as three sub-methods of one screen, so the four rows rest on one experiment per partner, not three.

BioPlex anti-tag co-immunoprecipitation in human HEK293T cells; the orthogonal method that corroborates the BLOC1S6 two-hybrid hit.

A proximity-labelling screen in K562 cells in which AGGF1 is a bait. It is the source of 634 of the 742 IntAct records for AGGF1 and of most of its 695 distinct partners, and of the GO:0042802 self-interaction row, which is an artefact of using a biotin-ligase fusion as bait.

Anti-tag co-immunoprecipitation in human U2OS cells; the orthogonal method supporting the AGGF1-MAB21L3 interaction.

Refutes the E133K-Klippel-Trenaunay association: 9 of 275 healthy white controls (3.3 percent) carry the variant, a frequency indistinguishable from that reported in cases.

The single overgrowth patient found to carry E133K inherited it from a clinically normal parent.

A second, independent population reporting E133K as a polymorphism rather than a disease mutation. Cited for its title claim only.

The originating laboratory's own follow-up, which concedes that the AGGF1-Klippel-Trenaunay relationship was not firmly established and moves to two different tagSNPs.

Zebrafish aggf1 knockdown causes defective vasculogenesis and angiogenesis and loss of venous identity markers; constitutively active AKT rescues it. This is the source of the zebrafish orthologue's own GO:0001525 IMP, which is what the human IBA row propagates from.

Zebrafish aggf1 acts upstream of scl, fli1 and etsrp in hemangioblast specification. Cited as corroboration for the vasculogenesis row, not as its evidence; no supporting_text is taken from it.

Purified AGGF1 induces autophagy in HUVECs dose-dependently, shown by LC3-II and p62 western blot, GFP-LC3 puncta and electron microscopy.

Autophagy is required for every angiogenic behaviour AGGF1 drives: both pharmacological inhibition and ATG5 knockdown abolish AGGF1-induced proliferation, migration, tube formation and aortic-ring sprouting.

AGGF1 treatment significantly induces HUVEC migration in scratch and Transwell assays.

Cited in prose only, as corroboration that AGGF1 activates PI3K p110alpha and p85alpha leading to AKT, GSK3beta and p70S6K activation. No annotation rests on it and no quote is taken from it.

The crystal structure of human DHX15 bound to the NKRF G-patch shows the motif running in an extended conformation across the helicase surface and tethering the catalytic core to the flexibly attached C-terminal domains.

G-patch binding increases DHX15's RNA affinity, helicase activity and ATPase activity - i.e. the domain is a helicase-activation module, not an autonomous nucleic-acid-binding module.

Immunostaining in human HCT116 cells places AGGF1 in the nucleus co-localised with p53. This is the best-documented nuclear localisation of the human protein and GO records none of it.

Serial deletion mapping localises p53 binding to residues 434-509, the FHA domain, and co-immunoprecipitation confirms the isolated FHA domain binds p53. No phosphatase control, phospho-site mutant or peptide competition was used, so this is not evidence that the FHA reads a phosphosite.

Of six COSMIC somatic FHA-domain variants tested, G437E, Q467H, Y469N and N483T impair AGGF1's tumour-suppressor activity while R447Q and V497I do not. G437 is the conserved glycine of the canonical phosphothreonine-anchoring G-R pair; R447 is not the conserved arginine (R438 is) and V497 lies outside the annotated FHA core.

AGGF1 moves from nucleus to cytoplasm in endothelial cells during angiogenesis, and the dynamic distribution is required for its angiogenic function. A nuclear localisation signal is mapped to residues 260-288.

Cytoplasmic distribution requires both the FHA domain and 14-3-3 alpha/beta, and the FHA domain is what binds 14-3-3. No phosphorylation claim is made in the abstract, and phospho-dependence was not tested.

Integrin alpha5beta1 is the endothelial receptor for AGGF1: GST-AGGF1 precipitates integrin alpha5 from HUVEC extracts dose-dependently, and only anti-alpha5, anti-beta1 and anti-alpha5beta1 antibodies block HUVEC adhesion to AGGF1.

AGGF1 treatment of HUVECs activates FAK, Src and AKT, and the AKT response is abolished by siRNA against ITGA5, ITGB1, PTK2 or SRC.

The angiogenic activity maps to residues 604-613 (FQRDDAPAS), a motif lying outside both the FHA and the G-patch domain, and the RDD is required - changing it to the classical RGD integrin motif abolishes blocking activity.

Reports an AGGF1-integrin alpha7 interaction via the RDDAPAS motif. The experiments were performed in mouse MOVAS-1 cells and in mice, so this would support ISO rather than IPI in human and is deliberately not used as evidence for the GO:0005178 proposal.

AGGF1 is a structural and regulatory component of paraspeckles, forming an outer rim around the NONO/PSF/PSPC1/NEAT1 core and controlling paraspeckle size and number.

RNA immunoprecipitation shows AGGF1 interacting with NEAT1 - the only direct measurement of RNA binding by this protein, and the basis for moving the GO:0003676 IEA row to GO:0003723.

AGGF1 regulates alternative splicing, decreasing the exon skipping/inclusion ratio in a CD44 minigene - a second, independent assay of the splicing activity characterised in PMID:40035560.

Reports that AGGF1 binding TWEAK reduces the TWEAK-Fn14 interaction in atrophic muscle - the opposite direction to PMID:39905000 in retinal endothelium. The discrepancy is recorded as a knowledge gap and neither direction is annotated.

Reports that AGGF1 enhances integrin alpha7 binding to LAP-TGF-beta1, blocking maturation of TGF-beta1. Cited in prose only; the work is in mice and no annotation rests on it.

Co-immunoprecipitation in human retinal microvascular endothelial cells independently re-confirms the AGGF1-TNFSF12 interaction first reported in 2004.

Silencing AGGF1 reduces TNFSF12-FN14 binding, i.e. AGGF1 promotes the interaction - the opposite of what PMID:36696895 reports in muscle.

AGGF1 protein is elevated in the vitreous fluid of patients with proliferative diabetic retinopathy, independent human evidence that the protein reaches the extracellular space.

Full-length transcriptome sequencing of human pulmonary artery endothelial cells with AGGF1 silenced shows AGGF1 regulating alternative splicing of 436 genes.

AGGF1 promotes skipping of SRSF6 exon 3 to produce full-length SRSF6, and full-length SRSF6 rescues the proliferation, migration and tube-formation defects of AGGF1-silenced endothelial cells.

A 2026 survey of the human G-patch family whose Table 3 lists AGGF1's interacting RNA helicase as Unknown, while naming DHX15 for CMTR1 and other members. This is the peer-reviewed state of the question the review's suggested experiment addresses.

Recombinant AGGF1 raises PI3K and phospho-Akt and improves blood-brain-barrier integrity after subarachnoid haemorrhage, and the protection is abolished by the PI3K inhibitor LY294002. Independent corroboration of the AGGF1-PI3K/AKT axis from a group with a senior author who appears on none of the dominant group's papers - but the work is in rats, so it supports the pathway without bearing on the human evidence code.

The AGGF1 effect is PI3K-dependent: the protective roles of recombinant AGGF1 are lost when PI3K is inhibited.

Immunofluorescence in human HCT116 cells shows AGGF1 co-localising with gammaH2AX after cisplatin-induced DNA double-strand breaks. Cited only as independent human-cell corroboration that AGGF1 is nuclear - gammaH2AX marks nuclear chromatin - and not for the DNA-repair interpretation, which this review does not annotate.

The cell system is human HCT116, the same line in which PMID:33069768 images nuclear AGGF1, but the work is from a different group.