Oncofusion

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Genemoderate confidence 3 of 5: One strong study, or several smaller consistent ones.Q86-pan-fusion-core2

WBP11 (Q9Y2W2) - a splicing activator in the pan-MLL-fusion core, isolated from its own partners, and a human haploinsufficiency gene

also called WBP11 · NPWBP · SIPP1 · SNP70 · WW domain-binding protein 11 · Npw38-binding protein · splicing factor that interacts with PQBP-1 and PP1

WBP11 helps the spliceosome cut introns out of new RNA, and losing one working copy of it causes heart, spine, kidney and limb birth defects in people. It co-purifies with every MLL fusion tested, but none of its usual partners came along with it.

The same thing, for a scientist

WBP11 (Q9Y2W2, 641 aa) is a pre-mRNA splicing activator that binds PQBP1 and protein phosphatase 1. In Skucha 2018 it co-purified with all seven MLL fusions with MLL-AF4 at p = 0.0078 (5|5), negative control 0|0, and it is the single most UNIFORM row in this tranche after NUP50 - every one of the seven baits between p = 0.0029 and 0.0090. Functionally it is well defined: loss of WBP11 causes retention of about 200 introns including multiple introns in TUBGCP6, collapsing gamma-TuRC and blocking centriole duplication; and heterozygous loss-of-function in humans causes cardiac, vertebral, tracheo-oesophageal, renal and limb defects with a matching mouse phenotype, while homozygous null mouse embryos die before E8.5. Its interactome partners are absent from the Skucha network - PQBP1, SNW1, PRPF19, CDC5L, PLRG1 all at no n - so this is an isolated recovery. UniProt's uncoded note places it in the nucleus with granular heterogeneous distribution, excluded from nucleoli, co-localised with SC35 and U2B, and associating with vimentin in the cytoplasm of dividing cells - and vimentin is one of the nine proteins this beat's dispatch deliberately deferred as a likely contaminant.

Go deeper
The Skucha row, stated in full

7 of 7 fusions. MLL-AF1p 0.0044 (5|5), MLL-AF4 0.0078 (5|5), MLL-AF9 0.0029 (13|8), MLL-CBP 0.0029 (3|17), MLL-EEN 0.0063 (12|9), MLL-ENL 0.0074 (7|8), MLL-GAS7 0.0090 (9|10); negative control 0|0 1. Every bait falls between p = 0.0029 and 0.0090 - a three-fold spread across seven structurally unrelated fusion proteins - and total spectra run only 10 to 21. This is the tightest row in the tranche. A constitutive association and a constitutive background both look like this; the 0|0 control argues for the former without settling it.

What WBP11 does, and it is unusually well defined

WBP11 is required for splicing: its loss causes retention of about 200 introns, including multiple introns in TUBGCP6, a central gamma-TuRC component, and the resulting rapid decline in TUBGCP6 protein is a large part of why WBP11 loss blocks centriole duplication. Several other splicing factors required for centriole duplication interact with WBP11 and are likewise required for TUBGCP6 expression 2. In humans, heterozygous predicted loss-of-function and damaging missense WBP11 variants across seven unrelated families cause overlapping cardiac, vertebral, tracheo-oesophageal, renal and limb defects; Wbp11-null mouse embryos die before E8.5 and heterozygous nulls are small with axial skeleton, kidney and oesophagus defects 3. So this is a dosage-sensitive developmental gene, which is the strongest bite-back in this entry.

Isolated, and the module verdict for this tranche

Are the RNA-processing members of this tranche a module, the way the CPSF pair is? Measured by this beat from the 960-protein table, 2026-09-21, and the answer is different for each of them.

proteinits own complex in the 960verdict
ZC3H18RBM7 (4/7), ZCCHC8 (4/7), SRRT/ARS2 (1/7), plus RNA-exosome core EXOSC4 (3), EXOSC5 (2), EXOSC8 (4), EXOSC9 (3)a real module - NEXT plus the exosome, missing only MTREX
SONSRSF11 (6), LUC7L2 (6), LUC7L3 (6), IK (6), DDX46 (6), PRPF4B (6), CHERP (5), AKAP8L (5), ARL6IP4 (5)a broad splicing cohort, but SRRM2 - SON's own speckle partner - is absent
SCAF11none. SCAF1, SCAF4 and SCAF8 are all absentisolated
GPATCH4none. DHX15 is absent, and so is every other G-patch proteinisolated
WBP11essentially none. PQBP1, SNW1, PRPF19, CDC5L, PLRG1 all absent; BCAS2 at 2/7 and PPP1CA at 1/7isolated

So the group is scattered, with one clear exception. The right summary is not 'the splicing machinery came along' but 'one RNA-surveillance module came along, one large splicing cohort came along without its scaffold pair, and three proteins came along alone'.

The vimentin note, which is worth flagging back to the coordinator

UniProt's uncoded subcellular-location note for Q9Y2W2 reads: 'Predominantly located in the nucleus with granular heterogeneous distribution. Excluded from nucleoli in interphase cells, distributed throughout cytoplasm in dividing cells. Colocalized with SC35 and U2B in the nucleus. In the cytoplasm, associates with the intermediate filament protein vimentin.'

VIM is one of the nine proteins the coordinator deliberately deferred from this beat as a likely cytoskeletal contaminant, and it is in the pan-fusion 42. WBP11's documented cytoplasmic partner is vimentin. That does not rescue VIM - a vimentin association in dividing cells is not a reason to think vimentin binds a nuclear fusion protein - but it does mean the VIM row and the WBP11 row are not independent observations, and anyone auditing the contaminant call should know that. Two of the ten proteins with a non-zero negative control are the ones a contaminant hypothesis would predict (ACTB 3|3), and VIM's control is clean (0|0), so the deferral was a judgement call and not a measurement.

Note also that the 'colocalized with SC35' statement must be read with care: the SC35 monoclonal antibody targets SRRM2, not SRSF2 (PMID 33095160), so 'SC35-positive' means 'in SRRM2-marked speckles'.

The splicing dependency in this disease is real and is a different protein

Alternative splicing is a real, validated dependency in this disease and that is the reason not to dismiss these rows. MBNL1 is consistently overexpressed in MLL-rearranged leukaemias, its loss impairs propagation of murine and human MLL-rearranged leukaemia in vitro and in vivo, it controls intron exclusion in DOT1L and SETD1A among others, and a small-molecule MBNL1 inhibitor achieves selective leukaemic cell death 4. MBNL1 itself is NOT in the Skucha 960 network at any n (checked by this beat, 2026-09-21), and neither is PTBP1. So the splicing dependency and the splicing interactome are, as far as anyone has looked, two separate observations about the same disease.

Facts and figures
uniprotQ9Y2W2
length AA641
accession resolutionResolved live 2026-09-21: gene_exact:WBP11 AND organism_id:9606 AND reviewed:true returns exactly ONE reviewed row, gene_primary WBP11, Q9Y2W2, WBP11_HUMAN, 641 aa, synonyms NPWBP SIPP1 SNP70. Matches Skucha's table. Registry checked per rule 88: no row for WBP11, NPWBP or SIPP1.
localizationNucleus and cytoplasm - UniProt Q9Y2W2, both UNCODED (no ECO evidence code), fetched 2026-09-21. Per the standing rule, an uncoded UniProt location is not a measurement, and it is recorded here as uncoded.
subnuclear localizationFrom UniProt's UNCODED note, verbatim: 'Predominantly located in the nucleus with granular heterogeneous distribution. Excluded from nucleoli in interphase cells, distributed throughout cytoplasm in dividing cells. Colocalized with SC35 and U2B in the nucleus. In the cytoplasm, associates with the intermediate filament protein vimentin.' So: speckle-associated and nucleolus-EXCLUDED, both uncoded. 'SC35' must be read as SRRM2, not SRSF2 (PMID 33095160). No primary imaging source for this was located by this beat.
localization shown for fusionNO - nobody has imaged WBP11 in any KMT2A-rearranged cell.
vimentin noteUniProt records WBP11 associating with vimentin in the cytoplasm of dividing cells. VIM is in the pan-fusion 42 and was deliberately deferred by this beat's dispatch as a likely cytoskeletal contaminant. The WBP11 and VIM rows are therefore not fully independent observations. VIM's own Skucha negative control is 0|0 (clean); ACTB's is 3|3 (not clean). Flagged for the coordinator rather than acted on.
shown for fusionCo-purification with all seven MLL fusions including MLL-AF4 in Jurkat (p = 0.0078); shRNA-screened against MLL-AF9 in MOLM-13, score unpublished. NO independent experiment ties WBP11 to any KMT2A fusion.
selectivityUNKNOWN - not named among the paper's controls and not known to be among the 40 re-screened. Human haploinsufficiency causes multi-organ birth defects, which is an independent argument against it as a target. Must not reach a target list.
functional screenFUNCTIONAL SCREEN. Supplementary Data 2 (file MOESM5) is the shRNA library for the negative-selection screen: 768 rows, 128 unique gene symbols, exactly six shRNAs per gene - counted by this beat on 2026-09-21. All 128 conserved interactors were screened in MLL-AF9-expressing MOLM-13 cells, and the paper says so in those words ('scoring of shRNA-induced effects upon knockdown of all 128 MLL-fusion interactors'). So this protein WAS functionally tested against an MLL fusion, which is more than a co-purification. But the per-gene result is published only as the heatmaps in Fig. 2c/2d, with no table of scores anywhere in the paper or its five supplementary files, so the outcome for this protein is not recoverable. Absence class for that number: measured-not-reported - an afternoon with the authors' source data would close it.
absence classnever-measured
absence class noteNo instrument has been pointed at WBP11 in a KMT2A-rearranged cell outside the two screen hosts. The MOLM-13 shRNA score is measured-not-reported. PRIDE checked: PXD009338 is the only relevant deposition.
graph contextWBP11 appears in ZERO node files before this entry (id listing over 1,900 nodes, 2026-09-21).
skucha 2018
{
  "bait": "MLL-AF4 (= KMT2A::AFF1)",
  "p_value": 0.00782,
  "spectral_counts": "5|5",
  "n_fusions_of_seven": 7,
  "negative_control_counts": "0|0",
  "per_bait": {
    "MLL-AF1p": "0.0044 (5|5)",
    "MLL-AF4": "0.0078 (5|5)",
    "MLL-AF9": "0.0029 (13|8)",
    "MLL-CBP": "0.0029 (3|17)",
    "MLL-EEN": "0.0063 (12|9)",
    "MLL-ENL": "0.0074 (7|8)",
    "MLL-GAS7": "0.0090 (9|10)"
  },
  "af4_spectral_rank_of_seven": 7,
  "index_bait_note": "p = 0.0078. The tightest row in the tranche: all seven baits between 0.0029 and 0.0090, total spectra 10-21.",
  "source": "analyses/skucha-mll-fusion-interactome/results.json, re-derived from the cached MOESM4 xlsx 2026-09-21; run.py re-run, both controls PASS"
}
complex membership
{
  "complex": "Spliceosome-associated; WBP11-PQBP1-PP1",
  "partners_in_the_960": {
    "BCAS2": 2,
    "PPP1CA": 1
  },
  "absent_from_the_960": [
    "PQBP1",
    "PPP1CC",
    "SNW1",
    "PRPF19",
    "CDC5L",
    "PLRG1",
    "WBP4"
  ],
  "reading": "Isolated. Its named partners are absent and the two proteins present are at 1-2 of 7 fusions, which is the weak private tail of the network rather than corroboration."
}
cell types and states
[
  "Jurkat (human T-ALL) - AP-MS host, nuclear lysate",
  "MOLM-13 (human MLL-AF9 AML) - shRNA screen host, six shRNAs, score unpublished",
  "human cultured cells - splicing and centriole duplication",
  "seven human families and Wbp11 mouse nulls - developmental phenotype",
  "no leukaemia cell outside the two screen hosts, and no B-lineage KMT2A::AFF1 cell"
]
bounded literature
{
  "query": "(WBP11[tiab] OR NpwBP[tiab] OR SIPP1[tiab]) AND (KMT2A[tiab] OR MLL[tiab] OR \"MLL-AF4\"[tiab] OR \"MLL-AF9\"[tiab] OR \"t(4;11)\"[tiab])",
  "querytranslation": "(\"WBP11\"[Title/Abstract] OR \"NpwBP\"[Title/Abstract] OR \"SIPP1\"[Title/Abstract]) AND (\"KMT2A\"[Title/Abstract] OR \"MLL\"[Title/Abstract] OR \"MLL-AF4\"[Title/Abstract] OR \"MLL-AF9\"[Title/Abstract] OR \"t 4 11\"[Title/Abstract])",
  "count": 0,
  "date": "2026-09-21",
  "tool": "NCBI esearch db=pubmed",
  "names_tried": [
    "WBP11",
    "NpwBP",
    "SIPP1",
    "SNP70",
    "PQBP1 (partner form, run separately)"
  ],
  "positive_control": "MEN1[tiab] AND the identical five-term clause returns 85.",
  "partner_level_query": "(PQBP1[tiab] OR \"WW domain binding protein 11\"[tiab]) AND the same KMT2A clause returns 0.",
  "complex_level_query": "(spliceosome[tiab] OR \"splicing factor\"[tiab] OR \"RNA splicing\"[tiab]) AND the same KMT2A clause returns 19 - NOT zero - dominated by MBNL1 and PTBP1, neither of which is in the Skucha network.",
  "bound": "Titles and abstracts only; supporting figures not searched. Cytogenetic term quoted; querytranslation shows 't 4 11'[Title/Abstract] with no injected [UID] term."
}
functionally screened in the source paper
{
  "_added": "king, cycle 48, 2026-09-21, after Q86 flagged that cycle-47 entries understate the record. Verified by me directly from the supplementary file, not from the paper's prose.",
  "screened": true,
  "library_symbol": "WBP11",
  "shrnas_for_this_gene": 6,
  "design": "Supplementary Table 6 / MOESM5 is 768 data rows, 128 unique gene symbols, EXACTLY 6 shRNAs each -- counted with openpyxl on 2026-09-21. Negative-selection RNAi screen in MLL-AF9-expressing MOLM-13.",
  "what_this_DOES_establish": "Every one of the 128 conserved MLL-fusion interactors, this protein included, was functionally tested against an MLL fusion. An entry saying 'nothing in the paper validates this prey' is true of BINDING and understates the record.",
  "what_this_does_NOT_establish": "A per-gene result. Scores are presented as heatmaps (Fig. 2c/2d) and no per-gene depletion value is tabulated, so for any individual gene the outcome is measured-not-reported. It is also MLL-AF9 MOLM-13, a myeloid line, not the index fusion and not B-lineage.",
  "absence_class_for_the_per_gene_score": "measured-not-reported"
}
How this could bite us back
  • WBP11 is dosage-sensitive in humans: one damaged copy causes cardiac, vertebral, tracheo-oesophageal, renal and limb defects. Any intervention lowering WBP11 in an infant is proposing a partial phenocopy of a congenital malformation syndrome.
  • Homozygous Wbp11 loss is embryonic lethal before E8.5 in mouse, so there is no dose at which this is a clean target.
  • Losing WBP11 causes ~200 intron-retention events; a phenotype in leukaemic cells would be near-impossible to attribute to a specific mechanism.
Still open
  1. WBP11's row is the tightest in this tranche across seven unrelated baits. Is that a constitutive association with the shared KMT2A N-terminus, or a constitutive background? Comparing it against the empty-vector spectra in PXD009338 at peptide level would separate the two with no new experiment.
  2. Does WBP11 depletion cause intron retention in KMT2A::AFF1 target genes? MBNL1 does exactly this for DOT1L and SETD1A, so the assay and the expectation both already exist.
  3. WBP11 heterozygous loss causes multi-organ birth defects in humans. Does it have a haematopoietic phenotype that nobody has looked for? Blood counts in the reported families would be a three-line answer.
  4. WBP11 and VIM both appear in the pan-fusion 42 and WBP11 associates with vimentin. Is the VIM row a passenger of the WBP11 row, or the reverse, or neither?
Every source behind this entry (4)
  1. E1moderate confidence 3 of 5: One strong study, or several smaller consistent ones.paper

    WBP11 co-purified with all seven Strep-HA-tagged MLL fusions expressed as single-copy transgenes in isogenic human Jurkat T-ALL cells; for MLL-AF4 (= KMT2A::AFF1) the combined p-value is 0.00782 with spectral counts 5|5 and a negative control of 0|0.

    MLL-fusion-driven leukemia requires SETD2 to safeguard genomic integrity. · Skucha A, Ebner J, Schmoellerl J, Roth M, Eder T, Cesar-Razquin A, Stukalov A, Vittori S, Muhar M, Lu B, Aichinger M, Jude J, Mueller AC, Gyorffy B, Vakoc CR, Valent P, Bennett KL, Zuber J, Superti-Furga G, Grebien F · Nature Communications 2018
    PMID 29777171DOI
    What this evidence cannot show

    SYSTEM: the AP-MS host is JURKAT, a human T-ALL line, while KMT2A::AFF1 disease is B-lineage infant leukaemia; a partner requiring a B-cell or infant proteome cannot appear here and a T-lineage partner can appear spuriously. The bait is a Strep-HA-tagged, SINGLE-COPY, doxycycline-induced transgene at an FRT/Flp cassette, not the endogenous fusion. Prey came from bulk nuclear lysate (buffer C420, 420 mM NaCl) after a single STREP-Tactin step, so co-purification is NOT evidence of a direct contact. INCLUSION RULE: the paper kept the top 300 interactions per bait by combined p-value rather than applying a p threshold (Methods, verbatim: "All the identified bait-prey pairs were ranked by the combined p-value. The 300 most significant interactions per bait were retained."). Measured by this beat from the cached MOESM4 xlsx on 2026-09-21: 545 of the 2,049 per-bait p-values in the table (26.6%) exceed 0.05; within the MLL-AF4 column alone it is 186 of 291 (63.9%), and that column's maximum p is 0.175. MEASURED BY THIS BEAT, 2026-09-21, from the cached MOESM4 xlsx: across all 42 pan-fusion proteins the MLL-AF4 column carries the LOWEST total spectral counts of the seven baits for 34 of 42, and is sixth or seventh for 40 of 42. That is a bait-level property (transgene expression, purification depth or the DDX5/DDX17 GLM normalisation), not a statement about any one prey, so a low MLL-AF4 count must not be read as a weaker association than the same protein's count under another bait. For WBP11 the MLL-AF4 total (10 spectra over two replicates) is rank 7 of the seven baits, against a maximum of 21 under another bait. All seven per-bait values, p (replicate spectral counts): MLL-AF1p 0.0044 (5|5); MLL-AF4 0.0078 (5|5); MLL-AF9 0.0029 (13|8); MLL-CBP 0.0029 (3|17); MLL-EEN 0.0063 (12|9); MLL-ENL 0.0074 (7|8); MLL-GAS7 0.0090 (9|10). SPECIFIC TO THIS PROTEIN: the tightest row in this tranche - all seven baits within a three-fold p range and 10-21 total spectra - which is what a constitutive association looks like and equally what a constitutive background looks like. WBP11's own interaction partners (PQBP1, SNW1, PRPF19, CDC5L, PLRG1) are all absent from the network, so nothing corroborates it at the complex level. SELECTIVITY: the paper's named non-selectivity controls are RFC1, SF3A3 and CCT3 - knockdown inhibited MLL-wild-type K562 and HL-60 as much as MOLM-13 - against MEN1 as the selective positive. Only 40 of the 128 ('the 40 candidate genes with the highest confidence') entered that MLL-r versus MLL-wild-type re-screen, and the paper does not list which 40. This protein is not named among the controls, but that is NOT evidence of selectivity: it is equally consistent with the protein never having reached the second screen. Recorded as unknown, and this entry must not be read as nominating a target. Values re-read from the cached xlsx on 2026-09-21 and cross-checked against analyses/skucha-mll-fusion-interactome/results.json, whose two controls (128 proteins shared by >=5 baits and 42 by all seven, both matching the paper; MEN1 present with all seven) both PASS on today's re-run.

    Evidence that argues against this (2)
    • IntAct has never curated this dataset, so no independent curator has re-examined these calls and no interactome-coverage metric built on IntAct can see them; the raw spectra at ProteomeXchange PXD009338 have not been reanalysed here. The authors themselves removed seven proteins from the shared set by hand as 'either frequently observed contaminants or ... not detected in human hematopoietic cell lines', which concedes that the rank cutoff lets contaminants through - and ACTB survived that filter, sitting in the pan-fusion 42 with a NON-ZERO negative control (3|3). Ten of the 42 carry a non-zero negative control: PSIP1 0|5, MCM2 0|2, ACTB 3|3, CSNK2A1 2|0, RUNX1 0|2, SF3A3 0|3, TCEB3 0|1, CHD4 2|2, SMARCC1 1|0, ZNF512 0|2 - counted by this beat from the xlsx neg_ctrl column, 2026-09-21. ProteomeXchange/PRIDE 2018
    • The paper states that 'more than one third of proteins in the network of conserved MLL-fusion protein interaction partners were identified as essential in recent genome-wide screens'. Abundance and essentiality both raise the odds of recovery in an AP-MS experiment, so membership in the conserved core is partly a statement about how much of a protein is present in a nucleus, not only about what it binds. Skucha A et al. 2018
  2. E2strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

    WBP11 is a pre-mRNA splicing factor required for centriole duplication: its loss causes retention of about 200 introns including multiple introns in TUBGCP6, a central gamma-TuRC component, with a rapid decline in TUBGCP6 protein, and several other splicing factors required for centriole duplication interact with WBP11 and are required for TUBGCP6 expression.

    WBP11 is required for splicing the TUBGCP6 pre-mRNA to promote centriole duplication. · Park EM, Scott PM, Clutario K, Cassidy KB, Zhan K, Gerber SA, Holland AJ · J Cell Biol 2020
    PMID 31874114DOI
    What this evidence cannot show

    Human cultured cells, 2020, J Cell Biol; depletion plus transcriptome analysis. Not haematopoietic, not a fusion system. The mechanism is specific and well controlled but the phenotype route (splicing -> TUBGCP6 -> centriole) is one of presumably several consequences of losing a splicing activator. Read from the abstract.

    Evidence that argues against this (1)
    • A protein whose loss causes ~200 intron retention events has pleiotropic downstream effects, so attributing any leukaemia phenotype to a specific WBP11 substrate would be unjustified; and the human germline phenotype (E3) is developmental and multi-organ rather than haematopoietic, which is where a leukaemia-relevant substrate would have shown up first. Martin EMMA et al. 2020
  3. E3strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

    Heterozygous predicted loss-of-function and predicted damaging missense WBP11 variants in seven unrelated human families cause overlapping cardiac, vertebral, tracheo-oesophageal, renal and limb defects; Wbp11 homozygous null mouse embryos die before E8.5, fewer heterozygous null mice survive than expected, and survivors are small with axial skeleton, kidney and oesophagus defects.

    Heterozygous loss of WBP11 function causes multiple congenital defects in humans and mice. · Martin EMMA, Enriquez A, Sparrow DB, Humphreys DT, McInerney-Leo AM, et al. · Hum Mol Genet 2020
    PMID 33276377DOI
    What this evidence cannot show

    Human genetics across seven families plus a CRISPR-Cas9 mouse null, 2020, Human Molecular Genetics, 34 authors. This is a developmental and VACTERL-type phenotype with no reported haematopoietic component in the abstract. Cited here for one thing - WBP11 is dosage-sensitive in humans, which bounds any therapeutic idea involving lowering it - and for nothing about leukaemia. Read from the abstract.

    Evidence that argues against this (1)
    • The absence of a reported blood phenotype in seven families with heterozygous WBP11 loss is weak evidence against a haematopoietic requirement at half dosage, but it is also an absence of testing rather than a negative result: these families were ascertained for congenital malformations, and nobody reports having looked at their blood counts. Park EM et al. 2020
  4. E4strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

    MBNL1, an alternative-splicing regulator, is consistently overexpressed in MLL-rearranged leukaemias, its loss impairs propagation of murine and human MLL-rearranged leukaemia in vitro and in vivo, it regulates intron exclusion in genes essential for MLL-rearranged leukemogenesis including DOT1L and SETD1A, and a small-molecule MBNL1 inhibitor achieves selective leukaemic cell death.

    MBNL1 regulates essential alternative RNA splicing patterns in MLL-rearranged leukemia. · Itskovich SS, Gurunathan A, Clark J, Burwinkel M, Wunderlich M, Berger MR, Kulkarni A, Chetal K, Venkatasubramanian M, Salomonis N, Kumar AR, Lee LH · Nat Commun 2020
    PMID 32398749DOI
    What this evidence cannot show

    Murine and human MLL-rearranged leukaemia; fusions not named in the abstract, so not specifically KMT2A::AFF1 or infant B-lineage. Cited only to establish that a splicing dependency in this disease exists. MBNL1 is NOT in the Skucha 960 network at any n. Read from the abstract.

    Evidence that argues against this (1)
    • The validated splicing dependency in this disease is a protein absent from the fusion interactome, and the splicing proteins that ARE in the interactome have no dependency data. The two lines of evidence do not currently meet. Skucha A et al. 2018
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