ELP2 (STATIP1/StIP1) - the double beta-propeller of the Elongator core, whose informal name collides with a different human gene and whose STAT3 function is a by-similarity annotation

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.

• ELP2 is not a therapeutic target and this entry must not be read as proposing one. It is a structural subunit with no catalytic activity, required for assembly of a complex that is required in nearly every DepMap line, and its loss-of-function human phenotype is severe childhood intellectual disability with spastic diplegia.
• The direction of effect across the whole Elongator field is tumour-suppressive - germline ELP1 loss predisposes to paediatric medulloblastoma, conditional Elp3 loss drives p53-mutant leukaemia/lymphoma in mice - so an agent inhibiting this complex in a leukaemia is predicted by the available data to point the wrong way.
• The identifier trap is a live reasoning hazard, not a curiosity. An agent asked to check ELP2's signalling role and searching the name on the record ('STAT3-interacting protein 1', StIP1) retrieves 273 records about STIP1/HOP and would conclude there is a rich literature. The name on a database record is not a search term.
• No ELP2-directed chemical matter exists, and the absence is recorded as UNMEASURED rather than zero: the ChEMBL activity endpoint returned HTTP 500 on three attempts on 2026-09-22, so no row count was obtained. An instrument failure is not a result.

1. Does human ELP2 interact with STAT3? UniProt asserts it at ECO:0000250 by similarity to mouse, the protein is still named STAT3-interacting protein 1, and this beat found no human experimental annotation - while the informal symbol that would find such a paper returns 273 records about a different gene. One co-IP would settle a twenty-four-year-old name.
2. Is ELP2's double beta-propeller a reader of anything? It is the same fold class as gene-wdr5, whose central channel binds an arginine and receives the KMT2A WIN motif, and no binding assay of any kind has been reported for the ELP2 propellers. A histone-peptide or methyl-arginine array on recombinant ELP2 is a one-week experiment with a clear negative interpretation.
3. Why is ELP2 at -0.63 when ELP5 is at -1.21, in an obligate complex? Within-complex essentiality spread is unexplained for Elongator and is the only place in these data with enough dynamic range for a selectivity question.
4. Is the nonsense-mediated-decay statement on ELP2's UniProt record true? It is ECO:0000305 curator inference, and 'an assembly-essential subunit of an obligate complex is produced at very low levels because of a premature stop codon' is a claim that a single RNA-seq or western would confirm or delete.
5. Does the Elongator complex appear in any curated IKK, STAT3 or JAK interactome? ELP1 and ELP2 were both named for such a pathway, and nobody has asked whether those preparations were capturing Elongator.

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

   ELP2 (Q6IA86, ELP2_HUMAN) is an 826-residue Elongator subunit built of fourteen annotated WD repeats forming two seven-bladed beta-propellers required for complex assembly, whose UniProt alternative names are SHINC-2 and STAT3-interacting protein 1 and whose gene synonym is STATIP1; its SUBUNIT comment asserts an interaction with STAT3 and JAKs at ECO:0000250 (by similarity to mouse Q91WG4) with no human experimental annotation, and it carries a DISEASE comment for autosomal-recessive intellectual developmental disorder 58.

   UniProtKB Q6IA86 (ELP2_HUMAN) - reviewed human record, length 826 aa · UniProt Consortium · UniProtKB 2026
   ▸What this evidence cannot show

   Accession resolved 2026-09-22 by gene_exact:ELP2 AND organism_id:9606 AND reviewed:true with gene_primary and length read back (rules 62, 65, 66): exactly one reviewed human row, primary gene name ELP2, entry ELP2_HUMAN, 826 aa, synonym STATIP1. Three evidence codes matter and are recorded rather than flattened: the FUNCTION comment is ECO:0000303 (author statement from a review, not an experiment); the DOMAIN comment describing the double beta-propeller is ECO:0000250:P42935, by similarity to YEAST Elp2; and the STAT3/JAK interaction is ECO:0000250:Q91WG4, by similarity to MOUSE. UniProt also carries a MISCELLANEOUS comment at ECO:0000305 (curator inference) that the protein may be produced at very low levels because of a premature stop codon causing nonsense-mediated decay.

   ▸Evidence that argues against this (1)

   • The two MRT58 natural variants on this record (residues 206 and 462) are both annotated 'uncertain significance' in UniProt's own variant table, which is a weaker statement than the DISEASE comment reads. The DISEASE comment rests on a single Case Reports paper describing two siblings. Cohen JS et al. 2015
2. E2established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.review

   Elongator consists of two copies each of ELP1-ELP6 organised into a catalytic ELP1/2/3 subcomplex and an accessory ELP4/5/6 subcomplex forming an assembly of about 850 kDa, with ELP3 as the catalytic subunit carrying a radical SAM domain and a PUTATIVE histone acetyltransferase domain.

   Structural insights into the function of Elongator. · Dalwadi U, Yip CK · Cell Mol Life Sci 2018
   PMID 29332244DOI
   ▸What this evidence cannot show

   A REVIEW, cited as a map of architecture and nomenclature only. The word 'putative' applied to the HAT domain is the review's own.

   ▸Evidence that argues against this (1)

   • Superseded in structural detail by cryo-EM of the fully assembled complex, which also reports biochemical characterisation of assembled HUMAN Elongator and shows the Elp456 module as a hetero-hexamer. Jaciuk M et al. 2023
3. E3established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.paper

   ELP2 is a component of the human ELP123 subcomplex whose cryo-EM structures bound to tRNA and cofactors resolve four stages of the wobble-uridine acetylation reaction at resolutions to 2.9 Angstrom.

   Cryo-EM structures of the human Elongator complex at work. · Abbassi NE, Jaciuk M, et al. · Nat Commun 2024
   PMID 38750017DOI
   ▸What this evidence cannot show

   Human, but the substrate throughout is tRNA - no histone, nucleosome or chromatin template anywhere in the series. Abstract read; full text not read. PDB identifiers 8PTX/8PTY/8PTZ/8PU0 were taken from the UniProt cross-reference list of Q6IA86 (which matches those of O95163 and Q9H9T3) and NOT read off the paper; no residue span in this entry was read off a deposit.

   ▸Evidence that argues against this (1)

   • A structure of ELP123 with tRNA cannot exclude a histone activity that was never assayed in the same preparation. No Elongator structure in any species has been solved with a histone tail or a nucleosome. Dalwadi U et al. 2018
4. E4strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

   StIP1 (STAT-interacting protein 1) and IKAP were both identified as subunits of the human Elongator complex when it was purified from HeLa extracts, where holo-Elongator has histone acetyltransferase activity against H3 and H4 and a three-subunit core form does not despite containing catalytic ELP3, and Elongator is a component of early elongation complexes formed in HeLa nuclear extracts that interacts directly with RNA polymerase II in solution.

   Purification and characterization of the human elongator complex. · Hawkes NA, Otero G, et al. · J Biol Chem 2002
   PMID 11714725DOI
   ▸What this evidence cannot show

   Biochemical purification from HeLa; abstract read, full text not read. This single paper is the origin of BOTH of this beat's name traps - it is the point at which StIP1 became ELP2 and IKAP became ELP1 - and neither protein's alternative-name field was retired afterwards. It is also the load-bearing HUMAN evidence that the small subunits are required for HAT activity, and it contradicts the contemporaneous three-polypeptide human purification on that exact point.

   ▸Evidence that argues against this (1)

   • The composition disagreement is unresolved: a human Elongator purified the same year comprised three polypeptides and DID have H3-directed HAT activity. Complex composition from a purification depends on tag, salt and cell type, so both subunit counts are properties of preparations. Kim JH et al. 2002
5. E5strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.database

   ELP2's informal name StIP1 is a retrieval trap in the opposite direction from a low-recall retired symbol: measured 2026-09-22 with one [tiab] tag per term and querytranslation read back, STATIP1[tiab] returns 1 record while StIP1[tiab] returns 273, of which only 14 of a sampled 150 titles mention STAT, JAK or Elongator - the bulk being STIP1, stress-induced phosphoprotein 1 (HOP), a different approved human gene that PubMed's case-insensitive index does not distinguish from StIP1.

   NCBI E-utilities esearch over PubMed with esummary title-checking, run 2026-09-22 by Q98 with querytranslation asserted non-empty on every call · Oncofusion knowledge-graph project (Q98-elongator-smyd3) · NCBI E-utilities 2026
   ▸What this evidence cannot show

   The 14-of-150 figure is a TITLE check on the 150 most recent of 273 records, not a full-text adjudication, so it is a lower bound on the on-topic fraction and an upper bound on precision - some ELP2 papers will discuss StIP1 in an abstract without a title hit. The point survives either way, because the contaminating records are a DIFFERENT GENE rather than a different field: STIP1/HOP appears in the titles with alpha-synuclein, prion protein, cardiomyocyte hypertrophy and ferroptosis. Not a rediscovery: data/symbol-collisions.json (120 rows, read before the first query as rule 88 requires) contains no row for ELP1, ELP2, ELP3, ELP5, ELP6, IKBKAP, SMYD3, Elongator, H3K14 or H4K8.

   ▸Evidence that argues against this (1)

   • The measurement does not establish that ELP2 has no STAT3 function; it establishes that the question cannot be asked through the informal symbol. UniProt's STAT3/JAK clause is ECO:0000250 from mouse, so the honest statement is that this beat found no HUMAN experimental annotation, having searched only the abstract index. UniProt Consortium 2026
6. E6moderate confidence 3 of 5: One strong study, or several smaller consistent ones.paper

   Compound-heterozygous missense variants in ELP2 were identified by whole-exome sequencing in two brothers with severe intellectual disability, spastic diplegia and self-injury whose diagnosis had eluded workup for over twenty years, establishing ELP2 as a gene implicated in neurodevelopmental disability.

   ELP2 is a novel gene implicated in neurodevelopmental disabilities. · Cohen JS, Srivastava S, et al. · Am J Med Genet A 2015
   PMID 25847581DOI
   ▸What this evidence cannot show

   A Case Reports paper describing TWO SIBLINGS from one family - n = 2, one genotype, no functional validation reported in the abstract - and UniProt annotates both variants 'uncertain significance'. Abstract read; full text not read. Cited as the basis of the DISEASE comment and for the field-vocabulary point, not as strong genetic evidence. Note the paper's own opening sentence describes Elongator as 'a multi-subunit protein complex essential to transcription elongation, histone acetylation, and tRNA modification' - a 2015 clinical restatement of the 2002 functional assignment, which is how the chromatin claim stays current without being retested.

   ▸Evidence that argues against this (1)

   • The claim that Elongator is 'essential to histone acetylation' in this paper's own framing is exactly what the current curated position disputes: UniProt now names human ELP3 a tRNA uridine(34) acetyltransferase and says protein-lysine acetyltransferase activity is unclear in vivo. A disease paper's introduction is not evidence about mechanism. Abbassi NE et al. 2024
7. E7strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.database

   No paper names ELP2 and a KMT2A fusion together: measured 2026-09-22 with one [tiab] tag per term and querytranslation read back, ELP2[tiab] AND KMT2A[tiab] = 0, AND MLL[tiab] = 0, AND leukaemia[tiab] = 0, AND leukemia[tiab] = 1 (a flow-cytometry MRD assay in which ELP2 is not this gene), and the mandatory complex form Elongator[tiab] AND KMT2A[tiab] = 0 and AND MLL[tiab] = 0, against positive controls through the identical shape of AFF1[tiab] AND KMT2A[tiab] = 104, DOT1L[tiab] AND KMT2A[tiab] = 30 and KMT2A[tiab] AND histone[tiab] = 218.

   NCBI E-utilities esearch over PubMed, run 2026-09-22 by Q98 with querytranslation asserted non-empty on every call · Oncofusion knowledge-graph project (Q98-elongator-smyd3) · NCBI E-utilities 2026
   ▸What this evidence cannot show

   Zero in TITLES AND ABSTRACTS ONLY; supporting figures and supplementary tables not searched (rule 80), which matters because a subunit appearing in a fusion proximity proteome would appear in a supplementary table. Name list searched: ELP2, STATIP1, StIP1, and the complex form 'Elongator' - the complex form is mandatory for a subunit absence (rule 64) and returns 0 against both KMT2A and MLL. INSTRUMENT ALARM RECORDED WITH THE RESULT. On the first pass of this beat's symbol sweep, ELP3[tiab] and ELP6[tiab] each returned a well-formed esearchresult with count 0, querytranslation EMPTY STRING, and errorlist and warninglist both {}. Re-run minutes later through the identical code path they return 202 and 43. Every count in this entry was therefore taken through a guarded wrapper that REFUSES any response whose querytranslation is empty and retries. A zero with an empty querytranslation is an instrument failure, not a result, and nothing else in the response says so.

   ▸Evidence that argues against this (1)

   • The repository-side check is the one that could have overturned this and did not: grepping this project's five KMT2A-fusion interactome analyses (mll-fusion-interactome-complexes, skucha-mll-fusion-interactome, interactome-coverage-on-rest, core-complex-interactome-gap, aff1-interactome-gap) for ELP1 through ELP6, Elongator and SMYD3 returns nothing at all. This project has previously declared a literature empty while citing the disproving paper in four other entries, so the grep is the check that matters. IntAct/EMBL-EBI 2026
8. E8moderate confidence 3 of 5: One strong study, or several smaller consistent ones.database

   IntAct REST returns 68 interaction records for ELP2 (Q6IA86) spanning 51 distinct molecules, which include ELP1, ELP2, ELP3, ELP4 and ELP6 but include NO POLR2A and none of KMT2A, MEN1, AFF1, AFF4, MLLT1, MLLT3, MLLT10, DOT1L, PSIP1, CDK9, ELL, KAT7, WDR5 or HOXA9 - so ELP2 is the only subunit of the catalytic ELP1/2/3 lobe with no curated RNA-polymerase-II contact of its own.

   IntAct molecular interaction database, REST endpoint findInteractions (not PSICQUIC) · IntAct/EMBL-EBI · IntAct 2026
   ▸What this evidence cannot show

   Queried 2026-09-22 through IntAct REST findInteractions and NOT PSICQUIC (rule 93), with the documented control findInteractions/Q03164 returning 376 records, so the endpoint is working. The POLR2A asymmetry is a statement about CURATION DEPTH and not about biology: ELP2 has 68 records to ELP1's 130 and ELP3's 107, so the missing Pol II record is at least as likely to reflect that fewer ELP2 experiments have been curated as to reflect a real difference in contact. Partner names were read from the moleculeA/moleculeB gene-symbol fields across paged results.

   ▸Evidence that argues against this (1)

   • An IntAct absence is 'measured-not-curated' for any partner that appears only in an uncurated proteome, and this project has already established that the index fusion's own AP-MS interactome (PMID 29777171) has never been entered into IntAct - so no IntAct-derived statement about a KMT2A-fusion partner can be complete. IntAct/EMBL-EBI 2026
9. E9moderate confidence 3 of 5: One strong study, or several smaller consistent ones.paper

   The only connection between the Elongator complex and any fusion oncoprotein runs through ELP3, which is phosphorylated on tyrosine by ALK, is phosphorylated in tumour cells expressing the oncogenic NPM-ALK fusion protein, has Tyr202 as the major ALK site, and whose Y202 phospho-mutant reduces cell growth and impairs gene expression when introduced into ALK-positive tumour cells.

   ELP3 Acetyltransferase is phosphorylated and regulated by the oncogenic anaplastic lymphoma kinase (ALK). · Li MT, Liang JY, et al. · Biochem J 2019
   PMID 31341009DOI
   ▸What this evidence cannot show

   Cited here only to establish that ELP2 is NOT the subunit with a fusion connection and to point the reader at gene-elp3; the full treatment, caveats and counter-evidence for this result live there. ALK-positive lymphoma cell lines; abstract read, full text not read.

   ▸Evidence that argues against this (1)

   • NPM1::ALK is a kinase fusion and KMT2A::AFF1 is a chromatin fusion, so 'a fusion oncoprotein phosphorylates an Elongator subunit' is analogous in form only. It does not transfer. Dalwadi U et al. 2018
10. E11moderate confidence 3 of 5: One strong study, or several smaller consistent ones.paper

    Human Elongator interacts directly with RNA polymerase II and facilitates Pol II transcription in a chromatin- and acetyl-CoA-dependent manner, with histone acetyltransferase activity specific to H3 and much weaker on H4.

    Human Elongator facilitates RNA polymerase II transcription through chromatin. · Kim JH, Lane WS, et al. · Proc Natl Acad Sci U S A 2002
    PMID 11818576DOI
    ▸What this evidence cannot show

    The purified complex 'was found to be composed of THREE polypeptides', so it cannot place ELP2 in the HAT-active species, and the contemporaneous six-subunit purification found a three-subunit core to have NO HAT activity. Abstract read; full text not read. Cited for the Pol II contact and the chromatin dependence, which are its robust content, and for ELP2's nuclear localisation call.

    ▸Evidence that argues against this (1)

    • Directly contradicted on composition-versus-activity by PMID 11714725. Two human purifications from 2002 disagree and neither histone assay has been repeated in human cells in the twenty-four years since. Hawkes NA et al. 2002
11. E12_HAT_YEASTestablished confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.paper

    In YEAST, intact Elongator is a histone H3 and H4 acetyltransferase whose predominant sites are H3K14 and H4K8, it acetylates core and nucleosomal substrates where isolated Elp3 is not specific, the three smallest subunits Elp4, Elp5 and Elp6 are REQUIRED for that HAT activity, and multiply-acetylated H3 and H4 are reduced in vivo in ELP3-null cells.

    Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo. · Winkler GS, Kristjuhan A, et al. · Proc Natl Acad Sci U S A 2002
    PMID 11904415DOI
    ▸What this evidence cannot show

    Saccharomyces cerevisiae throughout - not human, not haematopoietic, not a fusion system (this project's rule that the system belongs in the claim, not only the caveat). Abstract read; full text not read. The in vivo arm is a chromatin immunoprecipitation of bulk acetylated H3/H4 in an ELP3 deletion, so it establishes that Elongator contributes to steady-state acetylation levels and not that Elongator is the writer at any named gene. The requirement for the small subunits is a requirement for HAT ACTIVITY OF THE COMPLEX and does not make ELP4, ELP5 or ELP6 catalytic.

    ▸Evidence that argues against this (1)

    • The same paper's own framing has been overtaken. UniProt's current human ELP3 record renames the protein 'tRNA uridine(34) acetyltransferase' and states that protein-lysine acetyltransferase activity is unclear in vivo; the 2018 structural review calls the ELP3 HAT domain putative. A 2002 yeast result is not withdrawn by a 2026 database opinion, but a beat that cites only this paper is quoting the high-water mark of a claim that has receded. Dalwadi U et al. 2018
12. E12_HAT_HUMANstrong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

    In HUMAN HeLa cells the purified Elongator complex exists in two forms and only the six-subunit holo-Elongator has histone acetyltransferase activity against H3 and H4: the three-subunit core form has NO HAT activity despite containing the catalytic ELP3 subunit, and Elongator is a component of early elongation complexes formed in HeLa nuclear extracts and interacts directly with RNA polymerase II in solution.

    Purification and characterization of the human elongator complex. · Hawkes NA, Otero G, et al. · J Biol Chem 2002
    PMID 11714725DOI
    ▸What this evidence cannot show

    Biochemical purification from HeLa; abstract read, full text not read. This is the paper that reassigned two proteins to Elongator - it identifies StIP1 (ELP2) and IKAP (ELP1) as subunits of the human complex - so it is simultaneously the source of the small-subunit requirement in human cells and the source of two of the identity traps recorded in this beat. It is ALSO the resolution of a disagreement this graph already records: gene-elp4 notes that a contemporaneous human purification recovered only three polypeptides WITH HAT activity (PMID 11818576) and leaves the disagreement open; this paper's three-subunit core has NO HAT activity. Both are 2002, both are human, and they disagree. Recorded as a live disagreement, not as a resolution in either direction.

    ▸Evidence that argues against this (1)

    • THE DIRECT CONTRADICTION, and it is not resolved. A human Elongator purified from HeLa the same year was composed of THREE polypeptides and DID have HAT activity specific to histone H3, facilitating Pol II transcription in a chromatin- and acetyl-CoA-dependent manner. Complex composition determined by purification depends on the tag, the salt and the cell type, so 'three subunits, no HAT' and 'three polypeptides, HAT' are both properties of preparations. No later human paper this beat could find repeats either HAT assay. Kim JH et al. 2002
13. E12_TRNA_NOWstrong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

    The current curated and structural position is that Elongator is a tRNA wobble-uridine modification enzyme: UniProt names human ELP3 'tRNA uridine(34) acetyltransferase' (EC 2.3.1.311) and states that its protein-lysine acetyltransferase activity is unclear in vivo, and every high-resolution structure of human Elongator is of the ELP123 subcomplex bound to tRNA and cofactors, resolving four stages of the U34 acetylation reaction with no histone in the series.

    Cryo-EM structures of the human Elongator complex at work. · Abbassi NE, Jaciuk M, et al. · Nat Commun 2024
    PMID 38750017DOI
    ▸What this evidence cannot show

    Cryo-EM to 2.9 Angstrom of human ELP123 with tRNA; abstract read, full text not read. An absence of histone in a structural series is not evidence that histones are not substrates - nobody put one in - so this bounds what the human structural work SHOWS and not what Elongator can do. The UniProt FUNCTION clause quoted here is coded ECO:0000269 to PMID 29415125 for the tRNA half, while the replacement catalytic activity and the EC number are ECO:0000250 BY SIMILARITY from a non-human ortholog: UniProt renamed the human protein on an inferred activity, which is worth knowing before quoting the new name as settled.

    ▸Evidence that argues against this (1)

    • ELP3 does demonstrably acetylate at least one non-histone PROTEIN in vivo: in Drosophila neurons ELP3 is necessary and sufficient to acetylate the ELKS-family protein Bruchpilot at presynaptic densities, with a structural and a neurotransmitter-release phenotype. So 'primarily a tRNA enzyme' is a statement about the dominant activity, not a demonstration that the GNAT pocket cannot take a protein substrate. Note also that UniProt cites this same paper for 'Not a major acetyltransferase of tubulin', a clause its abstract does not contain - read the body before quoting that negative. Miśkiewicz K et al. 2011
14. E15weak confidence 2 of 5: Preliminary, small, indirect, or not yet peer reviewed.dataset

    ELP2 shows no KMT2A-selective dependency in this project's own DepMap scan: mean Chronos -0.7023 in 11 KMT2A-rearranged lines against -0.6304 in 43 other leukaemia lines, difference -0.0719, at a pan-essentiality of -0.6273 across 1208 lines and selectivity rank 2123 of 17,728.

    DepMap CRISPR (Chronos) gene-effect scan of 11 KMT2A-rearranged versus 43 other leukaemia lines (this project's own genome-wide scan, analyses/depmap-kmt2a-selective-scan-full) · Oncofusion knowledge-graph project · analyses/depmap-kmt2a-selective-scan-full/results.json 2026
    ▸What this evidence cannot show

    Joined 2026-09-22 from analyses/depmap-kmt2a-selective-scan-full/results.json (generated 2026-09-19T10:12:06Z). NOT re-fetched and NOT independent of that scan: every caveat it carries applies, including that the 11 KMT2A-rearranged lines come from nine individuals and that the arm is myeloid-enriched, so a difference there mixes fusion status with lineage. The scan records a generation timestamp and NOT a DepMap RELEASE, which is this project's rule-83 exposure carried forward rather than fixed here. Read the numbers by this project's own DepMap rules: a rank is not an effect size, a difference is not a dependency, the anti-selective half is 50 percent of any gene set by construction with this graph's base rate at 45.3 percent, and a gene depleted this deeply across all lines is FLOOR-COMPRESSED - there is almost no dynamic range left in which selectivity could appear, so a small arm-to-arm difference is uninterpretable rather than small. The screen is also leukaemia lines only.

    ▸Evidence that argues against this (2)

    • A difference of -0.0719 at a pan-essentiality of -0.627 across 1208 lines is floor-compressed and uninterpretable, not small: a gene required in nearly every line has no dynamic range left in which KMT2A selectivity could show. Reporting the rank would be reporting the null. Oncofusion knowledge-graph project 2026
    • ELP2 is the second-shallowest of the six subunits at -0.627 (against ELP5 -1.209, ELP1 -1.022, ELP6 -0.981, ELP3 -0.965, ELP4 -0.459), which is the one place in the DepMap data where a subunit has enough dynamic range for a selectivity question to be askable at all - and the answer there is still -0.072, indistinguishable from zero. The within-complex spread is itself unexplained for an obligate assembly. Oncofusion knowledge-graph project 2026

• part of →ELP1 (IKBKAP/IKAP) - the Elongator scaffold that was first named for the IKK complex, is a paediatric-cancer predisposition gene, and has an RNA Pol II contact in IntAct

  both in the catalytic ELP1/2/3 lobe of Elongator; ELP2 double beta-propeller required for assembly, ELP1 the scaffold

• part of →ELP4 (PAXNEB) - a required subunit of Elongator, the one partner of the seven with a genuine histone-acetyltransferase connection, and the one whose fusion supplies only its last 43 residues

  subunits of the same six-protein Elongator complex, in the catalytic and accessory lobes respectively

• analogous to →WDR5 — the partner that is not a partner: it binds the half of KMT2A the fusion throws away

  same fold class - seven-bladed WD40 beta-propeller - but ELP2 has no reported histone or methyl-arginine binding, where WDR5 is this graph canonical reader and the KMT2A WIN-motif receptor

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

  BOUNDED ABSENCE: 0 literature records, 68 IntAct records with no KMT2A-axis partner AND no POLR2A, absent from all five fusion-interactome analyses in this repo

• related to →Plain-English: what transcription elongation is, and why a traffic light explains this leukemia

  subunit of the complex named for elongating Pol II - but ELP2 is the catalytic-lobe subunit with NO curated POLR2A contact of its own

• ← part ofELP3 - the catalytic subunit, the only Elongator protein with a real acetyltransferase domain, and the one whose loss in mouse blood causes marrow failure and then p53-mutant leukaemia

  both in the catalytic ELP1/2/3 lobe of Elongator