Re-bound at full text: 40 records pair an ENL alias with condensate and phosphorylation language, 11 of them congress abstract books, and none tests whether YEATS reader binding or ENL condensate behaviour is phosphorylation-gated
also called Q115 ENL condensate phospho re-bound
Whether adding a phosphate switches the ENL protein's ability to read histone marks or to form droplets has never been tested, and reading whole papers rather than summaries does not change that. A quarter of what the search returns are conference programmes.
The same thing, for a scientist
The entry records **0** abstract-level records for `(ENL OR MLLT1 OR YEATS1 OR LTG19) AND condensate-terms AND phospho-terms` and 9 for `YEATS domain x phospho`, none on topic. At full text the three-way intersection returns **40** and `YEATS domain x phosphorylation` returns **375** against an operand of 654 for `YEATS domain` [E1]. **All 40 were read: 11 are congress abstract books and the rest are reviews plus the ENL condensate literature itself.** The primary papers present are the ones the phase-2 dossier already rests on - **PMID 36272410** (*Mol Cell* 2022, hotspot mutations in the structured ENL YEATS domain link aberrant transcriptional condensates and cancer), **PMID 31853060** (*Nature* 2020, impaired cell fate through gain-of-function mutations in a chromatin reader) and **PMID 34174329** (*J Mol Biol* 2022, the intrinsically disordered proteins MLLT3 and MLLT1 as multimodal transcriptional switches) - **and none of them is a phospho-regulation experiment** [E1]. A 2026 addition, **PMID 42268713** (*Cell Rep*), reports the **MLLT3** YEATS domain binding acylation marks and 7SK RNA, which is the closest anyone has come to a regulated YEATS reader and is about the paralogue [E2]. **The absence survives.**
| script | none - Europe PMC BODY: queries, 2026-09-22 |
|---|---|
| status | run |
| verdict | SURVIVES at full text |
| entry re bounded | absence-enl-yeats-and-condensate-phospho-gating |
| absence class | never-measured |
| absence class basis | UNCHANGED. A phospho-gating experiment that was never performed leaves no deposit; PhosphoSitePlus, which could show whether the relevant residues are phospho-acceptors at all, returns HTTP 403 from this environment (see ana-q115-phosphositeplus-answers-403-to-its-own-homepage). |
queries — the numbers behind the chart
[
{
"q": "(MLLT1 OR YEATS1) AND condensate terms AND phospho terms",
"hits": 40,
"read": 40,
"on_topic": 0,
"proceedings": 11
},
{
"q": "\"YEATS domain\" AND (phosphorylation OR phosphorylated)",
"hits": 375,
"screened": false
},
{
"q": "\"YEATS domain\"",
"hits": 654,
"role": "operand control"
}
]primary papers in the hit list and why each is not the answer
[
{
"pmid": "36272410",
"why": "hotspot YEATS mutations and condensates - no phospho arm"
},
{
"pmid": "31853060",
"why": "gain-of-function chromatin-reader mutations - no phospho arm"
},
{
"pmid": "34174329",
"why": "a review of MLLT3/MLLT1 as intrinsically disordered switches"
},
{
"pmid": "42268713",
"why": "MLLT3 YEATS binds acyl marks and 7SK RNA - the paralogue, and RNA not phosphate"
}
]- The phase-2 ENL YEATS dossier assumes the reader pocket is constitutively available. If binding turns out to be phospho-gated, a competitive pocket inhibitor's apparent potency would depend on the signalling state of the cell, and a cell-line IC50 measured in one growth condition would not transfer to a patient's marrow.
- Are any of the ENL YEATS hotspot residues in PMID 36272410 known phospho-acceptors? That is a sequence lookup against a PTM database and would tell you whether the question is even well-posed - and the PTM database this beat tried is blocked.
- Does the MLLT3 YEATS-7SK interaction of PMID 42268713 have an ENL counterpart, and is it phospho-sensitive? 7SK release is phosphorylation-controlled, so this is the most promising reframing of the entry's question.
- The 375-record YEATS-domain-x-phosphorylation intersection was never screened. It is the obvious place a phospho-dead YEATS mutant would be buried.
- E1strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.database
At full text, MLLT1/YEATS1 crossed with condensate terms and phosphorylation terms returns 40 records of which 11 are congress abstract books and none is a phospho-regulation experiment; YEATS domain crossed with phosphorylation returns 375 against a YEATS-domain operand of 654.
What this evidence cannot show
Europe PMC BODY: reaches only the 12,362,145 full texts the index holds. A congress abstract book is one document holding thousands of unrelated abstracts and matches almost any conjunction; across this beat's 18 fully-read intersections 83 of 321 records (25.9%, range 0-50%) are proceedings. Screening was at TITLE level unless a paper is listed as opened. The 375-record YEATS-domain-x-phosphorylation intersection was NOT screened; only the 40-record three-way set was. 'Phosphorylation' co-occurring with 'YEATS domain' in 375 of 654 YEATS papers mostly reflects that phosphorylation is named in almost any chromatin paper, which is why the three-way form is the bound.
Evidence that argues against this (1)
- A phospho-dead or phospho-mimetic YEATS point mutant tested inside a larger structure-function paper would be a supporting panel with no condensate word near it, and neither the three-way nor the two-way query reaches that. PMID 36272410 is a hotspot-mutation paper and its mutant panel was not inspected for phospho-site positions; if a hotspot residue is a known phospho-acceptor the entry's framing needs revisiting. Molecular Cell 2022
- E2moderate confidence 3 of 5: One strong study, or several smaller consistent ones.paper
A 2026 Cell Reports paper reports that the MLLT3 (AF9) YEATS domain binds H3K9/18/27 acetyl and crotonyl marks and the 7SK noncoding RNA, linking transcription and RNA signalling in haematopoiesis - the nearest thing to a regulated YEATS reader, and it concerns the paralogue rather than ENL.
The MLLT3 YEATS domain binds histone marks (H3K9/18/27ac/cr) and ncRNA (7SK), linking transcription and RNA signaling to regulate hematopoiesis. · Cell Reports 2026What this evidence cannot show
TITLE-CHECKED ONLY, from the full Europe PMC record. RNA binding is not phosphorylation, so this does not answer the entry's question; it is recorded because a second input to YEATS reader function changes what 'gating' could mean and because 7SK is already a node-worthy object in this graph through P-TEFb.
Evidence that argues against this (1)
- 7SK is the scaffold of the inhibitory P-TEFb snRNP, whose release IS phosphorylation-controlled. If the MLLT3 YEATS domain binds 7SK, then YEATS reader function may be coupled to a phospho-regulated RNA switch indirectly - which would make the entry's question ill-posed rather than unanswered, and would be a more interesting result than either. Cell Reports 2026
SURVIVES at full text: 40 records read, 11 proceedings, and the three primary YEATS condensate papers contain no phospho arm
the sequence lookup that would tell you whether the YEATS hotspot residues are phospho-acceptors needs the PTM database that is blocked from this environment