NUP214 / CAN - the cytoplasmic-face nucleoporin that CRM1 docks against, and the 3' partner of four leukaemia fusions

This is a prediction, not a measurement. No one has seen this protein in this shape. The colours say how much the software trusts itself, and that is worth reading before anything else — the orange stretches are places the model is effectively saying this part has no fixed shape.

• NUP214 is common-essential, so any strategy aimed at the wild-type protein has no window; strategies must target the fusion junction, the CRM1 interaction or downstream output.
• The FG repeats are an intrinsically disordered, low-complexity docking surface with no pocket - the least tractable class of target by small molecule.

1. Does the FG-repeat count set the strength of HOXA activation as well as the strength of export blockade? SQSTM1-NUP214 retains 14 repeats and still upregulates clustered HOXA genes, which would let a dose-response be drawn across the three fusions.
2. Is the CRM1 pre-binding at HOXA and HOXB a property of the leukaemic cell or of the lineage? The eLife work shows it in LOUCY and not K562 or HL60, but never in a normal thymocyte.
3. NUP214 is common-essential, yet these leukaemias tolerate losing one allele to the deletion. What is the haploinsufficiency margin, and does it create a vulnerability?

1. E1established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.database

   Human NUP214 is UniProt P35658, 2,090 aa, primary gene name NUP214 with synonyms CAIN, CAN and KIAA0023; its annotated architecture comprises a seven-bladed beta-propeller at aa 41-404, a coiled coil at aa 680-1209 containing leucine zippers at 740-768 and 861-882, and an FG-repeat region annotated as 44 F-G repeats spanning approximately aa 236-1418 plus the C-terminal repeat tract.

   UniProtKB P35658 (NU214_HUMAN), Nuclear pore complex protein Nup214 / Protein CAN, 2090 aa · UniProt 2026
   ▸What this evidence cannot show

   Fetched live 2026-09-20 with gene_primary read back and length asserted (brief rules 62-65). UniProt's FG-repeat annotation is a computed repeat call and the published count of 44 FG repeats comes from the primary literature, not from this record; the two agree here but the record is the weaker source for that number.

   ▸Evidence that argues against this (1)

   • SOURCE-TYPE DEFEATER, specific to what this entry uses the record for. UniProt's coiled-coil, leucine-zipper and FG-repeat calls are annotations, and the functionally decisive surface of NUP214 in this graph is not among them: the CRM1-contacting motifs were defined by MUTATION, not by repeat detection - mutating the CRM1 motifs that contact NUP214 abolishes self-renewal in colony assays and prevents leukaemia over 300 days. That surface is a property of the CRM1 side of the interface and has no coordinate in the NUP214 feature table. Reading the domain map as though it located the oncogenic function would put the emphasis on the FG tract, which is the part the annotation is most confident about and the part with the least functional mapping in a leukaemia context. Aumann WK et al. 2021
2. E2moderate confidence 3 of 5: One strong study, or several smaller consistent ones.review

   Four NUP214 fusions occur in leukaemia - SET-NUP214, DEK-NUP214, SQSTM1-NUP214 and NUP214-ABL1; three retain the FG domain, with SET-NUP214 and DEK-NUP214 conserving 42 of 44 FG repeats and SQSTM1-NUP214 only 14, and the shorter FG fragment correspondingly produces less nuclear accumulation of protein and polyA+ RNA; SET-NUP214 is primarily associated with ALL and DEK-NUP214 exclusively with AML.

   NUP214 in Leukemia: It's More than Transport. · Mendes A, Fahrenkrog B · Cells 2019
   PMID 30669574DOI
   ▸What this evidence cannot show

   A review. Cited as a map of fusion architecture; the FG-repeat counts and the export-blockade comparison come from the primary reports it cites. Full text read via Europe PMC (PMC6356203). The claim that DEK-NUP214 is exclusively AML is a statement about the literature as of 2019.

   ▸Evidence that argues against this (1)

   • A 2025 review of NUP214 in AML states that SET-NUP214 does occur in AML, formed either by del(9)(q34.11q34.13) or a balanced t(9;9)(q34;q34), and that its prognostic impact in AML is not known - so the ALL/AML split is a tendency, not a rule. Bruserud Ø et al. 2025
3. E3strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

   In the human T-ALL line LOUCY, ChIP-seq shows CRM1 selectively bound at the HOXA and especially the HOXB cluster regions, absent from K562 and HL60; knockdown of SET-Nup214 down-regulates HOX genes but does NOT significantly reduce the amount of CRM1 bound at HOX regions, indicating that CRM1 functions as the recruiter of SET-Nup214 rather than the reverse.

   Chromatin-bound CRM1 recruits SET-Nup214 and NPM1c onto HOX clusters causing aberrant HOX expression in leukemia cells. · Oka M, et al. · eLife 2019
   PMID 31755865DOI
   ▸What this evidence cannot show

   Human leukaemia cell lines (LOUCY, MEGAL, K562, HL60, HEL), not patients and not the index disease. The order-of-recruitment conclusion rests on a knockdown that lowers but does not eliminate the fusion, so residual fusion could in principle still hold CRM1. Full text read via Europe PMC (PMC6874418).

   ▸Evidence that argues against this (1)

   • PUBLISHED CONFLICTING RESULT FROM THE SAME GROUP, four years later. The one-way recruitment model - CRM1 is prebound, the fusion docks onto it, knocking the fusion down does not move CRM1 - is hard to hold alongside the same laboratory's later report that the phase-separated nuclear bodies of SET::NUP214 promote the CONDENSATION of MLL1 together with CRM1 and co-localise with them on chromatin. A fusion that concentrates CRM1 into bodies is doing something to CRM1's distribution, which is the thing the knockdown was read as excluding. The knockdown was also partial by the authors' own description, so residual fusion could hold residual CRM1 and the two results may simply be measuring different pools. Oka M et al. 2023
4. E4moderate confidence 3 of 5: One strong study, or several smaller consistent ones.database

   In the DepMap CRISPR (Chronos) gene-effect data served by the Open Targets Platform, NUP214 is flagged essential with a mean gene effect of -1.12 across 1,208 cell lines, alongside XPO1 at -2.14 (essential), while MEN1 (-0.36), DOT1L (-0.15), KMT2A (-0.21), SET (-0.29) and HOXA9 (-0.17) are not flagged essential.

   DepMap CRISPR gene effect via Open Targets Platform GraphQL API (depMapEssentiality) · Open Targets / DepMap 2026
   ▸What this evidence cannot show

   Fetched 2026-09-20. The DepMap release version is NOT stated in the API response, so the release is unverified - the same limitation this project's existing DepMap analyses record. A mean over all lineages is not a lineage-split result and must not be read as a selectivity claim (brief: a DepMap number is not a result until it is lineage-split). Critically, NEITHER LOUCY NOR MEGAL is present in this dataset, so none of these numbers is measured in a SET-NUP214 context.

   ▸Evidence that argues against this (1)

   • PUBLISHED CONFLICTING RESULT, and it is about the instrument rather than this fetch. The MEN1 value in this very list is the demonstration: a mean Chronos gene effect of -0.36, not flagged essential, for the protein whose pharmacological inhibition produced a 22.8% CR+CRh rate (95% CI 12.7 to 35.8) in centrally confirmed KMT2A-rearranged relapsed/refractory acute leukaemia in AUGMENT-101 phase 2, with an overall response rate of 63.2%. A pooled pan-lineage gene effect and a genotype-selected clinical response are measuring different things, and where they have both been measured they disagree. Quoting NUP214 at -1.12 and MEN1 at -0.36 side by side invites the reading that NUP214 matters three times as much, which this data cannot support. Issa GC et al. 2025
5. E5established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.database

   On GRCh38, SET (ENSG00000119335) occupies chr9:128,683,424-128,696,400 and NUP214 (ENSG00000126883) chr9:131,124,868-131,234,667, both on the plus strand, so the two genes are 2,428,468 bp apart and the interstitial deletion that fuses them removes about 2.43 Mb.

   Ensembl REST lookup for ENSG00000119335 (SET) and ENSG00000126883 (NUP214), GRCh38 · Ensembl 2026
   ▸What this evidence cannot show

   Fetched live 2026-09-20; display_name read back on each record to confirm the id resolved to the intended gene (this project has had an Ensembl id resolve to the wrong gene). Gene-body coordinates, not breakpoint coordinates - the actual deletion endpoints lie inside SET's 3' region and NUP214 intron 17/18, so 2.43 Mb is the inter-gene gap and an upper bound on what is removed, not the measured deletion size in any patient.

   ▸Evidence that argues against this (1)

   • PUBLISHED CONFLICTING RESULT on scope. A single inter-gene distance describes the canonical cryptic del(9)(q34) and not the lesion class: array CGH, RT-PCR and Sanger sequencing across nine NUP214-rearranged acute leukaemias recovered DEK::NUP214, SET::NUP214 and NUP214::ABL1, of which only DEK::NUP214 is visible by chromosome banding. Different 5' partners on different chromosomes cannot share a 2.43 Mb interstitial gap, and even within SET::NUP214 the deletion endpoints are patient-level facts that no gene-body coordinate pair fixes. The number is a correct calculation about two gene records and should not be read as a measured deletion size. Brunetti M et al. 2024
6. E_q91_nup214_loc1established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.database

   UniProtKB P35658 (NU214_HUMAN, primary gene NUP214, 2,090 aa, read back live 2026-09-21) carries exactly ONE subcellular location value, 'Nucleus, nuclear pore complex', on ONE experimental attribution, ECO:0000269 PubMed:8108440, with a single location note reading 'Cytoplasmic side of the nuclear pore complex' (same attribution). No second value, no by-similarity call, no molecule- or fragment-scoped comment.

   UniProtKB P35658 SUBCELLULAR LOCATION comments, evidence codes and feature table, fetched live 2026-09-21 (one location value and one note, both from the founding paper) · UniProt Consortium · UniProtKB 2026
   ▸What this evidence cannot show

   One citation for one of the largest nucleoporins is thin on its face, and it is thin for a good reason: the question was settled in 1994 and has not needed revisiting. Note what the record does NOT carry - none of the four leukaemic fusion products has a molecule-scoped location comment here, although their compartments are published and are radically different from the wild type's.

   ▸Evidence that argues against this (1)

   • The absent fragment-scoped comments are the defect worth naming, and this project has the exact precedent. Rule 91 records that KMT2A's UniProt entry carries separate location comments for the taspase1 N320 and C180 cleavage products, and that filtering on ECO:0000269 discards both. NUP214 has the opposite problem: the fusion species exist, their compartments are published in leukaemia cell lines, and the record contains NO scoped comment at all - so a reader taking P35658 as the answer for a t(6;9) blast would place DEK::NUP214 at the nuclear pore when it is in nucleoplasmic bodies. A one-value record can be complete for the wild-type protein and badly wrong for the disease. Port SA et al. 2016
7. E_q91_nup214_loc2established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.paper

   The founding observation, and it is precisely the fact UniProt cites it for: partial amino-acid sequencing of a rat nucleoporin reacting with wheat-germ agglutinin and the polyspecific monoclonal antibody 414 revealed high similarity to the human CAN protein, and the paper establishes that THE HUMAN CAN PROTEIN, A PUTATIVE ONCOGENE PRODUCT ASSOCIATED WITH MYELOID LEUKEMOGENESIS, IS A NUCLEAR PORE COMPLEX PROTEIN THAT FACES THE CYTOPLASM. The abstract states that CAN's subcellular localisation HAD NOT PREVIOUSLY BEEN ESTABLISHED.

   The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm. · Kraemer D, Wozniak RW, Blobel G, Radu A · Proc Natl Acad Sci U S A 1994
   PMID 8108440DOI
   ▸What this evidence cannot show

   1994; the sequencing was on the rat orthologue and the identification is by similarity to the published human CAN cDNA, with the localisation established for the nucleoporin. Read from the abstract.

   ▸Evidence that argues against this (1)

   • Worth recording as a positive control on this tranche's method rather than as a dispute. Fifteen of the sixteen entries in this beat were checked for the rule-91 pattern - a compartment cited to a paper that is not about it - and hits were found repeatedly. NUP214 is the case where the check comes back clean: one value, one citation, and the cited paper's TITLE is the annotation. That the same procedure produces both outcomes is the argument that the procedure is discriminating rather than merely sceptical, which matters because this project has repeatedly built over-flagging instruments. UniProt Consortium 2026
8. E_q91_nup214_loc3strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

   The fusions form NUCLEAR BODIES, and the observation is ENDOGENOUS in leukaemia cells: SET-NUP214 NUCLEAR BODIES CONTAINING THE NUCLEAR EXPORT RECEPTOR CRM1 WERE OBSERVED IN THE LEUKAEMIA CELL LINES LOUCY AND MEGAL. Over-expression of SET-Nup214 in HeLa cells forms similar nuclear bodies that recruit CRM1, export cargo proteins and certain nucleoporins, and concomitantly affect nuclear protein and poly(A)+ RNA export. SQSTM1-Nup214, although mostly cytoplasmic, also forms nuclear bodies and inhibits nuclear protein but not poly(A)+ RNA export. The interaction of the fusion proteins with CRM1 is RanGTP-dependent by co-immunoprecipitation.

   The Oncogenic Fusion Proteins SET-Nup214 and Sequestosome-1 (SQSTM1)-Nup214 Form Dynamic Nuclear Bodies and Differentially Affect Nuclear Protein and Poly(A)+ RNA Export. · Port SA, Mendes A, Valkova C, Spillner C et al. · J Biol Chem 2016
   PMID 27613868DOI
   ▸What this evidence cannot show

   LOUCY is T-ALL and MEGAL is a leukaemia line; neither is KMT2A-rearranged and neither is B-lineage infant disease (rule 73). The mechanistic dissection is in HeLa over-expression, and the endogenous observation is imaging in two lines.

   ▸Evidence that argues against this (1)

   • The differential between the two fusions is the part that resists a simple model. SET-Nup214 affects both nuclear protein AND poly(A)+ RNA export; SQSTM1-Nup214 inhibits protein export but NOT RNA export, and is mostly cytoplasmic while still forming nuclear bodies. So body formation, protein-export blockade and RNA-export blockade are three separable properties, and this entry's existing claim that the amount of FG repeat retained tracks the degree of export blockade is a single-axis summary of a phenomenon with at least three axes. SQSTM1-NUP214 retains 14 of 44 FG repeats against SET/DEK's 42 and still makes bodies. Mendes A et al. 2019
9. E_q91_nup214_loc4strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

   The fusion bodies are CRM1-DEPENDENT AND PHARMACOLOGICALLY REVERSIBLE IN BOTH DIRECTIONS: SET-NUP214 and DEK-NUP214 both disturb the localisation of proteins essential for nucleocytoplasmic transport, particularly for CRM1-mediated protein export; ENDOGENOUS AND EXOGENOUS SET-NUP214 AND DEK-NUP214 FORM NUCLEAR BODIES; these bodies DISPERSE UPON TARGETED INHIBITION OF CRM1 and the two fusion proteins RE-LOCALISE THROUGHOUT THE NUCLEOPLASM; and the bodies REESTABLISH SHORTLY AFTER REMOVAL OF CRM1 INHIBITORS. Cell viability, metabolism and proliferation of leukaemia cell lines harbouring SET-NUP214 and DEK-NUP214 are compromised by CRM1 inhibition.

   Targeted CRM1-inhibition perturbs leukemogenic NUP214 fusion proteins and exerts anti-cancer effects in leukemia cell lines with NUP214 rearrangements. · Mendes A, Jühlen R, Martinelli V, Fahrenkrog B · Oncotarget 2020
   PMID 32934780DOI
   ▸What this evidence cannot show

   Leukaemia cell lines, not primary patient material, and not KMT2A-rearranged. CRM1 inhibitors have broad effects on nucleocytoplasmic transport, so dispersal of the bodies is not by itself evidence that CRM1 is the structural scaffold rather than one of several requirements.

   ▸Evidence that argues against this (1)

   • Reversible dispersal is usually read as evidence for a dynamic, liquid-like body, and this graph's standing condensate rule says that reading is not available from this experiment. Loss of a required multivalent client can dissolve a condensate AND can equally dissolve a cluster of proteins tethered to clustered binding sites - and here the rival model is not hypothetical, because CRM1 pre-binding at HOX and HOXB clusters in LOUCY is a published spatially clustered binding site that this entry already cites as its E3. Neither 1,6-hexanediol nor conventional FRAP would separate the two, and calibrated half-bleaching has not been applied to these bodies in anything retrieved. Oka M et al. 2023
10. E_q91_nup214_loc5strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

    A NUCLEOPORIN FUSION RELOCALISES MLL1 - the analogy the PI asked for, running toward this graph's own protein. NUP98 and NUP214 form chimeric fusion proteins that assemble into PHASE-SEPARATED NUCLEAR BODIES CONTAINING CRM1, and the nuclear bodies of NUP98::HOXA9 AND SET::NUP214 PROMOTE THE CONDENSATION OF MIXED LINEAGE LEUKEMIA 1 (MLL1), the histone methyltransferase essential for maintenance of HOX gene expression. These nuclear bodies are ROBUSTLY ASSOCIATED WITH MLL1/CRM1 AND CO-LOCALIZED ON CHROMATIN. Whole-genome chromatin-conformation capture shows NUP98::HOXA9 inducing a drastic alteration in high-order genome structure at target regions, with generation of chromatin loops and rearrangement of topologically associating domains, IN A PHASE-SEPARATION-DEPENDENT MANNER.

    Phase-separated nuclear bodies of nucleoporin fusions promote condensation of MLL1/CRM1 and rearrangement of 3D genome structure. · Oka M, Otani M, Miyamoto Y, Oshima R et al. · Cell Rep 2023
    PMID 37516964DOI
    ▸What this evidence cannot show

    The MLL1 here is WILD-TYPE KMT2A, not a KMT2A fusion, and the driving lesions are NUP98::HOXA9 and SET::NUP214 - so this is a statement about what a nucleoporin fusion does TO MLL1, not about what a KMT2A fusion does. Rule 73: not infant B-lineage KMT2A::AFF1. The phase-separation dependence is asserted from the assays this field standardly uses, which this graph's condensate rule says cannot distinguish LLPS from clustered-site binding.

    ▸Evidence that argues against this (1)

    • The symmetry this invites - nucleoporin fusions condense MLL1, therefore MLL1 fusions might condense in the same way - should be resisted on a concrete difference. In this system the CONDENSING AGENT is the FG-repeat-bearing nucleoporin fusion and MLL1 is the recruited client; in KMT2A::AFF1 the fusion's disorder is contributed by AFF1's pSER region and there is no FG repeat anywhere, and this graph's own endogenous MLL-AF4 imaging entry (localization-endogenous-mll-af4-punctate-negative) records a NEGATIVE for punctate distribution. The result establishes that MLL1 CAN be driven into a body by a sufficiently multivalent partner, which is a statement about MLL1's condensability under a strong external driver rather than evidence about what the index fusion does. Mendes A et al. 2020
11. E_q91_nup214_loc6strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

    A chromatin-level localisation of a NUP214 fusion in primary disease, with a pharmacological dependency: DEK::NUP214 from t(6;9)(p22.3;q34.1) defines a WHO-recognised separate disease entity in younger AML patients; a multi-omics comparison of 57 primary AML samples (whole-genome and targeted sequencing, transcriptomics, and drug screening with over 500 compounds) found t(6;9) cases display a SELECTIVE RESPONSE TO XPO1 INHIBITORS (selinexor and eltanexor) and a distinct transcriptomic signature of FOXC1 and HOX overexpression; CUT&RUN demonstrated DIRECT BINDING OF DEK::NUP214 TO THE PROMOTERS OF FOXC1 AND THE HOXA/HOXB CLUSTERS; and both the expression of those genes and the BINDING of DEK::NUP214 to their regulatory regions were SELECTIVELY REDUCED UPON XPO1 INHIBITION in t(6;9) cells.

    DEK::NUP214 acts as an XPO1-dependent transcriptional activator of essential leukemia genes. · Kaya F, Bewicke-Copley F, Miettinen JJ, Casado P et al. · Leukemia 2025
    PMID 40204893DOI
    ▸What this evidence cannot show

    AML with t(6;9), not KMT2A-rearranged disease and not infant B-lineage (rule 73). The 57-sample cohort is the comparator set; t(6;9) is rare, so the index arm within it is small and the abstract does not state its size.

    ▸Evidence that argues against this (1)

    • This is the strongest available argument that the nuclear bodies are functional rather than decorative, and it also supplies the reason not to transfer the therapeutic logic to this graph's disease. XPO1 inhibition works here because the fusion's chromatin occupancy is XPO1-dependent - the fusion reaches HOXA/HOXB through CRM1. KMT2A::AFF1 reaches HOXA through menin, LEDGF and the CxxC domain's direct CpG contact, none of which requires XPO1, so the shared HOXA phenotype and the shared sensitivity of some leukaemias to selinexor do not imply a shared mechanism. This graph holds gene-xpo1 and an XPO1 chromatin-bound-versus-soluble entry, and this result belongs there as a contrast rather than as support. Oka M et al. 2019

• ← bindsXPO1 / exportin-1 (CRM1) - the cell's main nuclear export receptor, and a chromatin-bound transcriptional scaffold

  XPO1 docks on NUP214 FG repeats at the pore and in the fusion

• ← part ofDEK::NUP214 is the sixth lesion on the XPO1 address - and the only one where the drug response was measured in primary patient cells

  the FG-repeat half of the fusion

• ← fuses withDEK - a chromatin architectural protein that gatekeeps H3.3 and boosts HP1alpha, is a fusion partner in its own right, and is the substrate behind this graph's third CK2 route

  DEK::NUP214, t(6;9)(p22.3;q34.1) AML; DEK contributes its N-terminal region

• related to →MEN1 / menin — the adaptor the fusion cannot work without

  the MEN1 value in this entry's own DepMap list (-0.36, not essential) is the demonstration that a pooled Chronos mean cannot see this graph's central dependency

• ← related toSUMO1 - not a complex partner of LEDGF but a modifier of it, and the interactome row cannot tell you which

  Both sit on the CYTOPLASMIC face of the nuclear pore complex - SUMO1 as the RanGAP1 conjugate on RanBP2 (PMID 9019411), NUP214 as a structural nucleoporin facing the cytoplasm (PMID 8108440). Neither is evidence about the other (Q91 2026-09-22)

• related to →Where SET::NUP214 actually is: mobile intranuclear bodies that trap CRM1, dissolve in mitosis and under CRM1 inhibitor, and reassemble on washout

  Wild-type NUP214 is on the CYTOPLASMIC face of the pore (PMID 8108440); SET-NUP214 and DEK-NUP214 form endogenous CRM1-containing NUCLEAR BODIES in LOUCY and MEGAL that DISPERSE on CRM1 inhibition and REFORM on washout (PMID 27613868, 32934780) (Q91 2026-09-22)

• related to →KMT2A / MLL1 — the gene that breaks

  A nucleoporin fusion relocalises wild-type MLL1: NUP98::HOXA9 and SET::NUP214 phase-separated nuclear bodies PROMOTE MLL1 CONDENSATION and are co-localized with MLL1/CRM1 ON CHROMATIN (PMID 37516964) - MLL1 as client, not driver (Q91 2026-09-22)

• related to →XPO1 / exportin-1 (CRM1) - the cell's main nuclear export receptor, and a chromatin-bound transcriptional scaffold

  DEK::NUP214 chromatin occupancy at FOXC1 and HOXA/HOXB by CUT&RUN is XPO1-DEPENDENT and is lost on XPO1 inhibition, alongside selective selinexor/eltanexor sensitivity in t(6;9) AML (PMID 40204893) (Q91 2026-09-22)

• related to →The case that the KMT2A-fusion condensate is an artefact — what 1,6-hexanediol, overexpressed tags and in-vitro droplets actually prove

  The NUP214-fusion bodies are reported as phase-separated and the evidence is dispersal on CRM1 inhibition - which cannot distinguish LLPS from binding to spatially clustered sites, and CRM1 pre-binding at HOX clusters IS such a site (Q91 2026-09-22)

• fuses with →SET::NUP214 (TAF-Ibeta-NUP214, SET-CAN), cryptic del(9)(q34.11q34.13) - a HOXA-driving fusion of a histone chaperone to a nucleoporin, with no KMT2A and no menin-binding motif

  NUP214 contributes the C-terminal FG-repeat region, 42 of 44 FG repeats

• co-occurs with →SET / TAF-I beta - a histone chaperone that binds the retained N-terminus of MLL, co-activates HOXA with it, and is itself a HOXA-activating fusion partner that recruits DOT1L

  the two partners of the del(9)(q34) fusion, 2.43 Mb apart on 9q34 (GRCh38: SET chr9:128,683,424-128,696,400; NUP214 chr9:131,124,868-131,234,667, both + strand)