Oncofusion

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Geneweak confidence 2 of 5: Preliminary, small, indirect, or not yet peer reviewed.Q136-interactome-tail-size-and-abundance

NFYC / NF-YC - a histone-fold transcription factor whose partner subunit carries an H2B-like ubiquitination, and the most selective of the eleven TF baits that reached KMT2A

also called nuclear transcription factor Y subunit gamma · NF-YC · CBF-C · NF-Y subunit C

NF-YC is one third of NF-Y, a protein that binds the CCAAT sequence found in a huge number of gene switches - and it does so using a fold borrowed from histones, the proteins DNA wraps around. Its partner subunit even carries the same kind of ubiquitin tag as histone H2B, which is the tag that licenses the H3K79 methylation this project measures.

The same thing, for a scientist

NFYC (HGNC:7806, ENSG00000066136, UniProt **Q13952**, 458 aa, 1p34.2) is the gamma subunit of **NF-Y**, the heterotrimeric CCAAT-box factor; NF-YB and NF-YC must dimerise before NF-YA can associate and the trimer can bind DNA [E4]. **NF-YB and NF-YC host histone-fold domains**: the crystal structure of NF-Y on a 25 bp CCAAT oligonucleotide shows the HFD dimer binding the DNA sugar-phosphate backbone **mimicking the nucleosomal H2A/H2B-DNA assembly**, and **NF-YB ubiquitination at Lys138 precedes and is equivalent to H2B Lys120 monoubiquitination** - so NF-Y is described by its own structural authors as a sequence-specific factor with nucleosome-like properties that **helps establish permissive chromatin modifications at CCAAT promoters** [E5]. That matters here because **H2BK120ub is the mark that licenses DOT1L's H3K79 methylation**, which this graph carries as `interface-dot1l-h2bub-ubiquitin`. NFYC enters the interactome on one row - IntAct **IM-28767**, **MI:1314 BioID**, **MI:1060 spoke**, **NFYC bait / KMT2A prey**, MI-score 0.27, HEK293 Flp-In [E1][E2] - and it is **the most selective of the eleven TF baits that reached KMT2A**: 49 preys, below the panel median of 58.5, ranking 57th of 102, giving **p = 0.084**, the lowest of any KMT2A-TF pair and NOT RESOLVED under the pre-registered threshold [E3]. **Nothing links NFYC to KMT2A or MLL in the literature under either operand** [E6].

Go deeper
The histone fold, which is the reason this entry is not just an eleventh row

Nardini et al. solved NF-Y bound to CCAAT DNA and reported three things that put NF-YC inside this project's subject matter rather than beside it 5:

  1. NF-YB and NF-YC are histone-fold-domain proteins. The HFD dimer contacts the DNA sugar-phosphate backbone, mimicking the nucleosome H2A/H2B-DNA assembly. NF-YA then inserts an alpha helix deep into the minor groove to read the CCAAT box.
  2. NF-YB is ubiquitinated at Lys138, and structural and mutational data indicate this precedes and is equivalent to H2B Lys120 monoubiquitination, the modification important in transcriptional activation.
  3. The authors' own conclusion: NF-Y helps establish permissive chromatin modifications at CCAAT promoters, and other HFD-containing proteins may work the same way.

H2BK120ub is the licensing mark for H3K79 methylation by DOT1L. This graph already carries interface-dot1l-h2bub-ubiquitin for that crosstalk, and the KMT2A fusion's central epigenetic output is H3K79me2 at its target genes. A factor that carries an H2B-equivalent ubiquitin on a histone-fold subunit, at CCAAT promoters, is in the same chemistry.

What this does NOT show, stated plainly. Nothing in this literature connects NF-Y to DOT1L, to H3K79, to KMT2A or to any fusion. NF-YB-K138ub being equivalent to H2BK120ub is a structural and mutational argument about a mark, not a demonstration that DOT1L reads it or that it licenses anything. The connection is a shared chemistry and a testable prediction, and this entry treats it as exactly that.

The interaction row - the best of a bad set, and still not good

One IntAct row, IMEx IM-28767: MI:1314 BioID, MI:1060 spoke, roles MI:0496 bait (NFYC) / MI:0498 prey (KMT2A), host taxid:9606(Homo sapiens HEK293flp-in embryonic kidney cell), MI-score 0.27 2.

What distinguishes it is bait selectivity. NFYC recovered 49 preys of the 946 in the BioID arm - below the panel median of 58.5 and ranking 57th of 102 baits, i.e. one of the narrower labellers. A narrow bait reaching a prey is more informative than a wide one reaching the same prey, and the both-margins null prices that in: p = 0.084, the smallest of the eleven KMT2A-TF pairs 3.

baitpreys recoveredp (KMT2A pair)
NFYC490.084
EN1700.123
NHLH1710.128
ELF2810.141
ELF1850.151
MYC1010.182
YY11290.236
KLF31410.260
NFIX1530.287
KLF121550.289
FEV1970.386

Read that table honestly: it is almost perfectly monotonic in bait width. The ordering of the eleven is essentially the ordering of how much each bait labelled, which is what a both-margins null is supposed to do, and it means none of these eleven rows carries pair-specific information. 0.084 does not clear the pre-registered PROMOTED threshold of 0.05 and would not survive correction for 62 tests. NFYC is first in line, not established.

The one leukaemia connection, and the subunit it is actually about

The connection is to NFYA, not NFYC, and this entry keeps that distinction. Yang et al. analysed alternative splicing by RNA-seq in AML cells from 341 patients against healthy CD34+ HSCs and found two main NFYA isoforms differing in exon 3 inclusion: NFYA-L and NFYA-S. Patients with NFYA-S predominance had more favourable characteristics and better outcomes after intensive chemotherapy independent of age and ELN risk, validated in TCGA; NFYA-L predominant cases, "as observed in KMT2A-rearranged leukaemia", were associated with relative chemoresistance 7.

So NF-Y has a documented association with KMT2A-rearranged AML - through the A subunit's splicing, in AML rather than infant ALL, as an observation rather than a mechanism. NFYC is the C subunit and is not the subject of that paper. It is recorded here because NF-YC and NF-YA are obligate partners in the same trimer (NF-YB/NF-YC must dimerise before NF-YA associates 4), so a shift in NF-YA isoform composition is a shift in the complex NF-YC sits in - but nothing measures NFYC in that cohort.

Granularity note. The PI's standing rule is one entry per thing. NFYA and NFYB are not written here and are named so the next beat finds them; whether the NF-Y trimer deserves a complex entry, and whether the NFYA splice result belongs in it, is a separate decision.

Localization, subnuclear compartment, cell type, and a bounded absence

Subcellular (UniProt): Nucleus, with no evidence code - uncoded, therefore a curator assertion and not a measurement 4.

Subnuclear (HPA immunofluorescence): nucleoplasm, main and only, reliability Supported; HPA additionally classes NFYC as an essential protein with molecular function activator and DNA-binding 8.

Structure. UniProt's feature table for Q13952 annotates no named domain - only a disordered region at 305-379 with low-complexity and polar-residue biases, and a long secondary-structure block of helices and strands across residues 40-117 from deposited crystallography 4. The histone fold is not in UniProt's feature table for this accession, so this entry sources it from the structural paper rather than from the database, and does not assert residue boundaries for it. Seven isoforms are annotated, several differing across 316-419.

Cell type of the observation: HEK293 Flp-In embryonic kidney, over-expressed tagged construct - not blood, not leukaemic, not KMT2A-rearranged. Cell state: proliferating immortalised line.

Other fusion families and the bounded absence. Run with scripts/pubmed_safe.py, both operands, translations recorded 6:

querytranslationn
(NFYC[tiab] OR NF-YC[tiab]) AND KMT2A[tiab]("NFYC"[Title/Abstract] OR "NF-YC"[Title/Abstract]) AND "KMT2A"[Title/Abstract]0
(NFYC[tiab] OR NF-YC[tiab]) AND MLL[tiab]("NFYC"[Title/Abstract] OR "NF-YC"[Title/Abstract]) AND "MLL"[Title/Abstract]0
control: (NF-Y OR NFYC OR NFYA OR NFYB)[tiab] AND (HOXA9 OR MLL OR KMT2A OR leukemia)[tiab]-29

Both zeros are genuine - non-empty translation, warninglist reading No items found. The control returns 29 records, so the family is not invisible to the instrument; it is NFYC specifically that has never been written about in connection with KMT2A or MLL under any spelling. Bounded by titles and abstracts only.

Other fusion families: nobody has looked. NFYC is not a fusion partner in any leukaemia this project tracks.

Facts and figures
hgnc IDHGNC:7806
symbolNFYC
ensembl gene IDENSG00000066136
uniprotQ13952
length AA458
chromosomal location1p34.2
entrez ID4802
identifier provenanceHGNC REST fetch/symbol/NFYC and UniProtKB Q13952 retrieved live 2026-09-23; Ensembl id taken from the HGNC record. HGNC lists no previous symbol. Both aliases were word-boundary matched against the full corpus id set and node text: NFYC is named in 3 node files, all enumerating the eleven TF baits; no entry existed under any spelling.
subnuclear location hpaNucleoplasm (main, reliability Supported, no additional location)
cell type of the observationHEK293 Flp-In embryonic kidney - not blood, not leukaemic, not KMT2A-rearranged
cell state of the observationover-expressed tagged construct, one isoform of seven, in a proliferating immortalised line
epigenetic roleINDIRECT BUT REAL AT THE COMPLEX LEVEL. NF-YB and NF-YC host histone-fold domains whose dimer binds DNA mimicking the nucleosomal H2A/H2B-DNA assembly; NF-YB is ubiquitinated at Lys138 in a modification reported to precede and be equivalent to H2B Lys120 monoubiquitination; the structural authors conclude NF-Y helps establish permissive chromatin modifications at CCAAT promoters. The ubiquitinated residue is on NF-YB, not NF-YC.
shown for fusionNO - nobody has looked at NFYC in any fusion. The proximity row is wild-type KMT2A in HEK293 Flp-In, and PubMed returns zero for NFYC against both KMT2A and MLL. The one NF-Y observation in KMT2A-rearranged leukaemia is about the NFYA subunit's splicing.
evidence classinteraction: single publication, single method, spoke-expanded BioID proximity, no orthogonal validation, and an ordering that is monotonic in bait width. Chemistry: a 2013 Cell crystal structure, read at abstract level, about the complex rather than this subunit.
prev and alias symbols
[
  "CBF-C",
  "NF-YC"
]
complex membership
{
  "complex": "NF-Y (CCAAT-binding factor), heterotrimer",
  "subunits": [
    "NFYA",
    "NFYB",
    "NFYC"
  ],
  "assembly_rule": "NF-YB and NF-YC must interact and dimerise before NF-YA can associate and the trimer can bind DNA",
  "histone_fold": "NF-YB and NF-YC both host histone-fold domains; the HFD dimer binds the DNA backbone mimicking the nucleosomal H2A/H2B-DNA assembly",
  "note": "NFYA and NFYB have no entry in this graph; named here so the next beat finds them rather than rediscovering them. Whether NF-Y deserves a complex entry is a separate decision."
}
interaction with project baits
[
  {
    "core_protein": "KMT2A",
    "core_uniprot": "Q03164",
    "partner_experimental_role": "bait",
    "core_experimental_role": "prey",
    "method": "MI:1314 proximity-dependent biotin identification",
    "expansion": "MI:1060 spoke",
    "mi_score": 0.27,
    "imex": "IM-28767",
    "pmid": "35140242",
    "host_cell": "HEK293 Flp-In embryonic kidney",
    "n_rows": 1,
    "n_publications": 1
  }
]
adjudication
{
  "verdict": "NOT RESOLVED",
  "p_pair_both_margins_held": 0.084,
  "rank_among_the_eleven_kmt2a_tf_baits": 1,
  "bait_preys_recovered": 49,
  "panel_median_preys_per_bait": 58.5,
  "bait_selectivity_rank_in_panel": "57 of 102 (1 = widest labeller)",
  "prey_baits_recovering_it": 11,
  "of_panel": 102,
  "honest_reading": "the ordering of all eleven KMT2A-TF pairs is essentially monotonic in bait width, so NFYC's first place is a fact about how much the NFYC construct labelled, not about KMT2A",
  "why_written_anyway": "NF-YB/NF-YC are histone-fold-domain proteins that bind DNA like H2A/H2B, and NF-YB carries a Lys138 ubiquitination reported equivalent to H2BK120ub - the mark that licenses DOT1L's H3K79 methylation",
  "source": "analyses/interactome-tail-size-and-abundance-adjudication/pair_null.json"
}
subcellular location uniprot
[
  "Nucleus (NO evidence code - uncoded annotation, not a measurement)"
]
bounded absence
{
  "queries": [
    "(NFYC[tiab] OR NF-YC[tiab]) AND KMT2A[tiab] -> 0",
    "(NFYC[tiab] OR NF-YC[tiab]) AND MLL[tiab] -> 0"
  ],
  "querytranslations": [
    "(\"NFYC\"[Title/Abstract] OR \"NF-YC\"[Title/Abstract]) AND \"KMT2A\"[Title/Abstract]",
    "(\"NFYC\"[Title/Abstract] OR \"NF-YC\"[Title/Abstract]) AND \"MLL\"[Title/Abstract]"
  ],
  "name_list_tried": [
    "NFYC",
    "NF-YC"
  ],
  "name_list_NOT_tried": [
    "CBF-C",
    "HAP5"
  ],
  "positive_control": "(NF-Y OR NFYC OR NFYA OR NFYB)[tiab] AND (HOXA9 OR MLL OR KMT2A OR leukemia)[tiab] -> 29",
  "bound": "titles and abstracts only; supporting figures not searched"
}
How this could bite us back
  • NF-Y binds one of the most common promoter elements in the genome and HPA classes NFYC as an essential protein. Any intervention against it is a genome-wide transcription intervention, which is the shape of a toxicity rather than a therapy.
  • The H2B-like ubiquitination is on NF-YB, not NF-YC. If this entry's chemistry argument ever became a rationale, the actionable subunit would be a gene that has no entry in this graph at all - which is a reason to write NFYB before acting on anything here.
  • The eleven-TF-bait ordering is monotonic in bait width. If a future beat cites NFYC's first place as evidence of specificity, it will be citing the labelling radius of a construct in a kidney cell, and this entry says so in its own adjudication field to make that hard to do.
Still open
  1. Is NF-YB Lys138 ubiquitination read by anything that reads H2BK120ub? The structural paper argues equivalence from geometry and mutation, and the obvious test - does a H2Bub reader module, or DOT1L itself, engage ubiquitinated NF-YB - appears never to have been done. If it does, a sequence-specific CCAAT factor carries a DOT1L-licensing mark to promoters, which would be a genuinely new route into the H3K79 axis. If it does not, the equivalence is structural only and this entry's main claim shrinks to a curiosity.
  2. Do KMT2A fusion target genes carry CCAAT boxes at rates above background? This is a motif scan against an existing fusion-occupancy dataset and costs an afternoon. A negative would close the NF-Y line cleanly; a positive would make the proximity row worth re-examining.
  3. Which NFYC isoform was the BioID bait? UniProt annotates seven, several differing across residues 316-419, and the deposition used one construct per bait. The question matters because NF-YC's C-terminal region is where the isoforms diverge and the histone fold is N-terminal.
  4. Does the NFYA-L / NFYA-S isoform ratio reported in KMT2A-rearranged AML also hold in KMT2A::AFF1 infant ALL, and does NFYC expression or isoform usage move with it? The published cohort is AML and the index disease is infant B-ALL.
Every source behind this entry (8)
  1. E1established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.paper

    Göös et al. identified 6,703 BioID and 1,536 AP-MS protein-protein interactions for 109 human transcription factors in HEK293 Flp-In cells; in the resulting IntAct deposition IM-28767, NFYC is one of eleven transcription-factor baits whose BioID neighbourhood contained KMT2A.

    Human transcription factor protein interaction networks. · Göös H, Kinnunen M, Salokas K, Tan Z, Liu X, Yadav L, Zhang Q, Wei GH, Varjosalo M · Nat Commun 2022
    PMID 35140242DOI
    What this evidence cannot show

    Abstract read; full text and supplementary tables not read. The eleven-bait set and the per-bait prey counts were re-derived from the deposition by this beat rather than quoted. All baits are over-expressed tagged constructs in embryonic kidney cells.

    Evidence that argues against this (1)
    • The paper reports 202 TF-TF interactions of which 118 involve NFI family members, which it describes as previously uncharacterised cross-talk. A screen in which one family accounts for more than half of all TF-TF contacts has a strong internal structure that this project's per-row reading does not account for. source 2022
  2. E2established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.database

    IntAct serves the NFYC-KMT2A record as PSI-MI MI:1314 proximity-dependent biotin identification, MI:1060 spoke expansion, NFYC experimental role MI:0496 bait and KMT2A MI:0498 prey, MI-score 0.27, host taxid:9606 Homo sapiens HEK293flp-in embryonic kidney cell, IMEx IM-28767, publication PMID 35140242.

    What this evidence cannot show

    Retrieved live 2026-09-23; 8,331 rows fetched against an endpoint-declared count of 8,331. Rule 93: PSICQUIC is a floor relative to IntAct REST and a REST query on this pair was not run. Spoke expansion means the binary pair was never measured. NFYC has seven annotated isoforms and the deposition used one construct per bait, so which isoform was tagged is unknown.

    Evidence that argues against this (1)
    • MI-score 0.27 is the deposition-wide value on every row in this arm and carries no pair-specific information. source 2026
  3. E3moderate confidence 3 of 5: One strong study, or several smaller consistent ones.dataset

    In IM-28767's BioID arm NFYC recovered 49 of 946 human preys, below the panel median of 58.5 and ranking 57th of 102 baits by reach, the narrowest of the eleven baits recovering KMT2A; under a null holding both margins NFYC recovering KMT2A has p = 0.084, the smallest of the eleven, and the ordering of all eleven is essentially monotonic in bait width (EN1 70 preys p=0.123, NHLH1 71 p=0.128, ELF2 81 p=0.141, ELF1 85 p=0.151, MYC 101 p=0.182, YY1 129 p=0.236, KLF3 141 p=0.260, NFIX 153 p=0.287, KLF12 155 p=0.289, FEV 197 p=0.386).

    What this evidence cannot show

    20,000 draws, seed 20260923. p = 0.084 does NOT clear the pre-registered PROMOTED threshold of 0.05 and would not survive Bonferroni over the 62 pairs tested (threshold 0.0008). The near-monotonicity of the ranking in bait width is stated because it is the honest reading: these eleven rows do not carry pair-specific information and the ordering is mostly an ordering of how much each bait labelled.

    Evidence that argues against this (1)
    • If the ordering is monotonic in bait width then it contains no information beyond bait width, and NFYC's first place is a fact about the NFYC construct's labelling radius or expression level in HEK293, not about KMT2A. This entry rests its case on the histone-fold chemistry instead. source 2026
  4. E4established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.database

    UniProt Q13952 is 458 aa and records NF-YC as a component of the sequence-specific heterotrimeric transcription factor NF-Y, which recognises the 5'-CCAAT-3' box and can act as activator or repressor depending on cofactors, with NF-YB and NF-YC required to interact and dimerise before NF-YA association and DNA binding (ECO:0000269, PMID 12401788 and PMID 23332751); subcellular location is given as Nucleus with no evidence code, and the feature table annotates no named domain, only a disordered region at 305-379 and deposited secondary structure across residues 40-117.

    What this evidence cannot show

    Fetched live 2026-09-23. The nucleus call is UNCODED and is therefore a curator assertion, not a measurement. The histone-fold domain is NOT annotated in this accession's feature table, which is why this entry sources it from the structural paper and asserts no residue boundaries for it. Seven isoforms are annotated with alternative sequence across 316-419 among others.

    Evidence that argues against this (1)
    • An obligate heterotrimer means no subunit has an independent activity. Any statement about 'NFYC does X' is really a statement about NF-Y, and a proximity row on the C subunit cannot distinguish the subunit from the complex. source 2026
  5. E5established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.paper

    NF-Y is composed of NF-YA and the NF-YB/NF-YC subunits, the latter two hosting histone-fold domains; the crystal structure of NF-Y bound to a 25 bp CCAAT oligonucleotide shows the HFD dimer binding the DNA sugar-phosphate backbone and mimicking the nucleosome H2A/H2B-DNA assembly, while NF-YA inserts an alpha helix deeply into the minor groove to make sequence-specific CCAAT contacts; structural and mutational data indicate NF-YB ubiquitination at Lys138 precedes and is equivalent to H2B Lys120 monoubiquitination, and the authors conclude NF-Y helps establish permissive chromatin modifications at CCAAT promoters.

    Sequence-specific transcription factor NF-Y displays histone-like DNA binding and H2B-like ubiquitination. · Nardini M, Gnesutta N, Donati G, Gatta R, Forni C, Fossati A, Vonrhein C, Moras D, Romier C, Bolognesi M, Mantovani R · Cell 2013
    PMID 23332751DOI
    What this evidence cannot show

    Abstract read; full text and structure coordinates not read, and no PDB id is recorded here because none was fetched. The Lys138 ubiquitination is on NF-YB, not on NF-YC - NFYC contributes the second half of the histone-fold dimer. The 'equivalent to H2BK120ub' claim is a structural and mutational argument, not a demonstration that any H2Bub reader engages it.

    Evidence that argues against this (1)
    • Nothing in this work connects NF-Y to DOT1L, to H3K79 methylation, to KMT2A or to any fusion. The link to this project's biology is a shared chemistry - an H2B-equivalent ubiquitin mark - and a shared vocabulary, and a shared vocabulary is exactly how this graph has previously let two unrelated facts harden into a mechanism. source 2013
  6. E6established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.database

    PubMed returns zero records for (NFYC OR NF-YC) AND KMT2A in titles and abstracts and zero for the same names against MLL, while the NF-Y family as a whole returns 29 records against HOXA9, MLL, KMT2A or leukemia.

    What this evidence cannot show

    Both zeros carry a non-empty querytranslation and a warninglist reading 'No items found.'. NAME LIST TRIED: NFYC, NF-YC. HGNC lists no previous symbol and gives CBF-C and NF-YC as aliases; CBF-C was not queried and is a plausible spelling in older literature. Bounded by titles and abstracts only; supporting figures not searched.

    Evidence that argues against this (1)
    • CBF-C was not in the name list. Rule 72's lesson is that a class absence is only as good as its name list, and this one is two names deep for a protein whose literature spans three naming conventions (NF-YC, CBF-C, HAP5 in the older comparative literature). source 2026
  7. E7moderate confidence 3 of 5: One strong study, or several smaller consistent ones.paper

    RNA-seq analysis of alternative splicing in AML cells from 341 patients against healthy CD34+ haematopoietic stem cells identified two main NFYA isoforms differing in exon 3 inclusion, NFYA-L and NFYA-S; NFYA-S predominance was associated with more favourable characteristics and better outcomes after intensive chemotherapy independent of age and European LeukemiaNet risk, validated in the TCGA cohort, while NFYA-L predominant cases, as observed in KMT2A-rearranged leukaemia, were associated with relative chemoresistance.

    Clinical relevance of NFYA splice variants in patients with acute myeloid leukaemia undergoing intensive chemotherapy. · Yang YT, Yao CY, Kao CJ, Chiu PJ, Lin ME, Hou HA, Lin CC, Chou WC, Tien HF · Br J Haematol 2024
    PMID 39192759DOI
    What this evidence cannot show

    Abstract read; full text not read. THIS IS ABOUT NFYA, NOT NFYC. The KMT2A-rearranged observation is a single clause in the abstract with no n, no effect size and no statistical test reported there, and it is an association between an isoform ratio and a leukaemia class, not a mechanism. The cohort is adult-inclusive AML, not infant ALL.

    Evidence that argues against this (1)
    • NFYA and NFYC are different genes on different chromosomes. Citing an NFYA splicing association in an NFYC entry is a subunit-level substitution, and this graph has a standing rule against exactly that kind of transfer for complexes. It is recorded because NF-YB/NF-YC dimerisation is obligate for NF-YA association, and it is explicitly NOT treated as evidence about NFYC. source 2026
  8. E8moderate confidence 3 of 5: One strong study, or several smaller consistent ones.database

    The Human Protein Atlas assigns NFYC a main subcellular location of nucleoplasm with no additional location, reliability 'Supported', classes it as an essential protein and a transcription factor, and gives its molecular function as activator and DNA-binding.

    What this evidence cannot show

    Antibody-based immunofluorescence in a small cell-line panel, not in leukaemic blasts. 'Supported' is the middle reliability tier. HPA's 'essential proteins' class is a gene-level annotation, not a KMT2A-selective dependency, and no DepMap figure for NFYC was fetched by this beat.

    Evidence that argues against this (1)
    • KMT2A's HPA main location is also nucleoplasm. Bait and prey sharing a compartment call is what makes a proximity row look informative when it is not, and it applies to all eleven of these TF rows equally. source 2026
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