ELP5 (DERP6) - the bridge that joins ELP3 to ELP4, the most essential Elongator subunit in DepMap, and a gene whose cytoplasmic call rests on an overexpression experiment

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.

• ELP5 is the worst therapeutic prospect in this beat on the essentiality axis: it is the deepest Elongator dependency in DepMap at -1.209 across 1,208 lines, which is an essential-function toxicity signal with no window rather than a target.
• The direction of effect for the complex is tumour-suppressive in the two best-evidenced systems - germline ELP1 loss predisposes to paediatric medulloblastoma and conditional Elp3 loss drives p53-mutant leukaemia/lymphoma in mice - so inhibiting Elongator through its assembly bridge in a leukaemia is predicted to point the wrong way.
• The one result that reads as pro-tumour - ELP5 depletion reducing melanoma migration and tumorigenicity - is RNAi in cell lines with no rescue reported, and it is the weakest of the three lineage results. It should not be used as a rationale.
• Losing Elongator function causes familial dysautonomia and neurodevelopmental disease in humans and destroys mouse haematopoiesis, so systemic inhibition of this complex has a known and severe phenotype rather than an unknown one, and the human phenotypes are paediatric.
• No ELP5-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 and no row count was obtained.

1. Does ELP5 loss destabilise Elongator more completely than ELP4 or ELP6 loss? ELP5 is the bridge that connects ELP3 to ELP4 and is the deepest DepMap dependency of the six at -1.21 against ELP4's -0.46, and nobody has compared the three accessory subunits' depletion for residual complex integrity. That 0.75-unit spread within an obligate complex is unexplained.
2. Does ELP5 loss change p53 output? Overexpressing DERP6 activated p53 transcriptional activity in a 2006 reporter assay that nothing has followed up, and loss of the catalytic subunit activates a p53-dependent checkpoint in mouse marrow. One western for p21 after ELP5 knockdown would either connect two orphan observations or delete one.
3. Where is endogenous ELP5? Both of its UniProt compartment calls are weakly sourced - one is an overexpression image, the other a paper whose abstract describes no localisation experiment - and no antibody-based localisation of endogenous human ELP5 was found by this beat.
4. Is ELP5's 'S-phase 2 protein' name based on anything? UniProt carries the alternative name and no cell-cycle function, annotation or GO term to support it. This is the third name in this beat that records a first hypothesis rather than a current one.
5. Is the 316-versus-300-residue divergence between the DERP6 paper's ORF and UniProt's canonical an isoform or an error? It is invisible to verify-accessions.py by construction.

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

   ELP5 (Q8TE02, ELP5_HUMAN) is a 300-residue Elongator subunit whose only annotated features are a disordered region at 264-300 and one phosphoserine, with Pfam PF10483 and no PDB entry; UniProt's alternative names are Dermal papilla-derived protein 6 and S-phase 2 protein, its gene synonyms are C17orf81 and DERP6, its SUBUNIT comment states it is required for optimal binding of ELP3 to ELP4, and its tissue-specificity comment (ubiquitous, high in heart, brain, liver, skeletal muscle and testis) is UNCODED.

   UniProtKB Q8TE02 (ELP5_HUMAN) - reviewed human record, length 300 aa · UniProt Consortium · UniProtKB 2026
   ▸What this evidence cannot show

   Accession resolved 2026-09-22 by gene_exact:ELP5 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 ELP5, entry ELP5_HUMAN, 300 aa. Evidence codes recorded: the FUNCTION comment's tRNA clauses are ECO:0000303 (author statement from a review); the cell-migration clause is ECO:0000250 (by similarity, mouse Q99L85); the SUBUNIT/bridge clause is ECO:0000269:22854966; the TISSUE SPECIFICITY comment carries NO evidence code at all; and two MISCELLANEOUS comments about isoforms are ECO:0000305 (curator inference). NOTE THE ALTERNATIVE NAME 'S-phase 2 protein': UniProt carries no cell-cycle function or annotation for ELP5, so that name asserts a cell-cycle role the record does not support - a third instance in this beat of a name recording a first hypothesis.

   ▸Evidence that argues against this (1)

   • An uncoded TISSUE SPECIFICITY comment is not a measurement by this graph's own standard (the finding that UniProt localisation is uncoded in 10.7% of entries here) - but in this case the measurement DOES exist, as a sixteen-tissue Northern blot in the DERP6 cloning paper, and only the evidence code is missing. That is the opposite of the usual defect and is the reason to open the paper rather than discard the line. Yuan J et al. 2006
2. E2strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

   DERP6 and C3ORF75 encode human ELP5 and ELP6; DERP6/ELP5 is required for the integrity of the Elongator complex and directly connects ELP3 to ELP4; and knockdown of DERP6/ELP5 or C3ORF75/ELP6 in melanoma-derived cells decreases migration, invasion and tumorigenicity, phenocopying depletion of Elongator through ELP1 or ELP3.

   DERP6 (ELP5) and C3ORF75 (ELP6) regulate tumorigenicity and migration of melanoma cells as subunits of Elongator. · Close P, Gillard M, et al. · J Biol Chem 2012
   PMID 22854966DOI
   ▸What this evidence cannot show

   The paper that established the identity of human ELP5 and ELP6, combining biochemistry with RNAi in melanoma-derived cell lines. Abstract read; full text not read. The phenotypic arm is siRNA/shRNA knockdown with migration, invasion and tumorigenicity endpoints - the class of experiment most exposed to off-target and incomplete-depletion artefacts - and no rescue is described in the abstract. UniProt cites this paper for ELP5's NUCLEUS localisation, and its ABSTRACT DESCRIBES NO LOCALISATION EXPERIMENT: it opens by asserting the field's compartment model (histone acetylation in the nucleus, tRNA modification in the cytoplasm) rather than measuring ELP5's compartment. Rule 91, defect direction, reported not edited.

   ▸Evidence that argues against this (1)

   • This is the ONLY result in which an Elongator subunit is REQUIRED for a cancer phenotype, and it is the weakest of the three lineage results: the medulloblastoma predisposition is human germline genetics with replication, the haematopoietic phenotype is mouse conditional knockout, and this is RNAi in melanoma cell lines. A beat wanting to write 'Elongator is required in cancer' would be quoting the weakest arm of a split literature. Waszak SM et al. 2020
3. E4weak confidence 2 of 5: Preliminary, small, indirect, or not yet peer reviewed.paper

   The human gene DERP6 - now ELP5 - was cloned from a testis cDNA library and mapped to 17p13.1, is ubiquitously expressed across sixteen adult tissues by Northern hybridisation with highest levels in heart, brain, liver, skeletal muscle and testis, was localised to the cytoplasm WHEN OVEREXPRESSED in cultured cells, and its overexpression activated the transcriptional activity of p53 in reporter assays.

   Cloning and characterization of the human gene DERP6, which activates transcriptional activities of p53. · Yuan J, Tang W, et al. · Mol Biol Rep 2006
   PMID 16850183DOI
   ▸What this evidence cannot show

   A 2006 gene-cloning and characterisation paper: Northern blot, OVEREXPRESSION localisation and a luciferase reporter, with no loss-of-function arm and no endogenous measurement of anything. Abstract read; full text not read. Two things are load-bearing and both are about how UniProt uses it. First, this paper is the ECO:0000269 source for ELP5's CYTOPLASM call, and its localisation is explicitly an overexpression result, which the UniProt record does not indicate - overexpressing a subunit of an obligate complex saturates its partners and produces a free pool whose compartment need not be the complex's. Second, the paper reports an ORF of 316 amino acids against UniProt's 300-residue canonical, which is the isoform-frame class this project's collision registry already records for C2CD3 and TMPRSS13 and which verify-accessions.py structurally cannot see.

   ▸Evidence that argues against this (1)

   • The p53 result points the OPPOSITE way from the haematopoietic one: here more ELP5 activates p53, while loss of Elp3 activates a p53-dependent checkpoint in mouse marrow. Two p53 observations fourteen years apart on two subunits, with opposite signs, one of them a reporter assay driven by overexpression. Recorded as a convergence worth one experiment and explicitly NOT as a pattern. Rosu A et al. 2021
4. E5strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

   IN MOUSE MODELS OF CONDITIONAL Elp3 INACTIVATION, loss of the catalytic Elongator subunit causes bone marrow failure by killing committing progenitors and compromises HSC grafting through a p53-dependent checkpoint, and after p53 deletion rescues haematopoiesis, loss of Elp3 prompts p53-mutated leukaemia/lymphoma with p53 and Elongator inactivation cooperatively promoting tumorigenesis.

   Loss of tRNA-modifying enzyme Elp3 activates a p53-dependent antitumor checkpoint in hematopoiesis. · Rosu A, El Hachem N, et al. · J Exp Med 2021
   PMID 33507234DOI
   ▸What this evidence cannot show

   Mouse, Elp3 and not ELP5, and not a KMT2A-rearranged system. Cited in THIS entry for the p53 convergence and to establish the direction of Elongator in blood; the full treatment lives in gene-elp3. The convergence with E4 is a shared word, not a shared mechanism, until somebody measures p53 output on ELP5 loss.

   ▸Evidence that argues against this (1)

   • The tumour phenotype is p53-conditional, so the tumour-suppressor reading is bounded. What survives unconditionally is that Elongator is required for normal haematopoietic differentiation and stem-cell grafting - which is already a reason not to inhibit the complex in a marrow disease. Waszak SM et al. 2020
5. E6strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.database

   No paper names ELP5 and a KMT2A fusion together: measured 2026-09-22 with one [tiab] tag per term and querytranslation asserted non-empty, ELP5[tiab] = 22, ELP5[tiab] AND KMT2A[tiab] = 0, AND MLL[tiab] = 0, AND leukemia[tiab] = 0, AND leukaemia[tiab] = 0, 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 and GEO DataSets, run 2026-09-22 by Q98 through a wrapper that refuses any response with an empty querytranslation · 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). Name list searched and MEASURED rather than assumed: ELP5[tiab] = 22, DERP6[tiab] = 3, C17orf81[tiab] = 1, and the complex form Elongator[tiab] = 608. The retired symbols add essentially nothing here, which is the ELP4 pattern rather than the ELP1 pattern - recorded as a negative so a later beat does not repeat it. ELP5's total literature is 22 records, so this is a small-literature absence and the correct reading is 'almost nobody has studied this protein', not 'people looked and found nothing'. 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)

   • Grepping this project's five KMT2A-fusion interactome analyses for ELP1 through ELP6, Elongator and SMYD3 returns nothing, which is the load-bearing half of the absence because this project has previously declared a literature empty while citing the disproving paper in four of its own entries. What is NOT bounded: 24 PRIDE projects mention Elongator (against a KMT2A control of 37) and none was opened project by project. IntAct/EMBL-EBI 2026
6. E7moderate confidence 3 of 5: One strong study, or several smaller consistent ones.database

   IntAct REST returns 37 interaction records for ELP5 (Q8TE02) spanning only 13 distinct molecules - the most sparsely curated of the six Elongator subunits - all of which are Elongator subunits, with no POLR2A and none of KMT2A, MEN1, AFF1, AFF4, MLLT1, MLLT3, MLLT10, DOT1L, PSIP1, CDK9, ELL, KAT7, WDR5 or HOXA9.

   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. WITH THIRTEEN DISTINCT PARTNERS THIS ABSENCE IS NEARLY VACUOUS and is recorded as such: a bait with 13 curated partners has not been looked at, so 'KMT2A is not among them' carries almost no information. It is included for completeness and because the recovery of all five sibling subunits confirms the query reached the right protein. Partner names read from moleculeA/moleculeB gene-symbol fields across paged results.

   ▸Evidence that argues against this (1)

   • An IntAct absence is 'measured-not-curated' for any partner appearing only in an uncurated proteome, and this project has established that the index fusion's own AP-MS interactome (PMID 29777171) has never been entered into IntAct. For a 13-partner bait that limitation dominates entirely. IntAct/EMBL-EBI 2026
7. E8established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.paper

   Elongator consists of two subcomplexes - Elp123 containing the enzymatically active Elp3 and the associated Elp456 hetero-hexamer - and cryo-EM of the fully assembled complex was solved in yeast at 4.3 Angstrom and in mouse at 5.9 Angstrom, with complementary mutational analyses in vitro and in vivo and biochemical characterisation of the assembled human Elongator, providing the molecular basis for assembly and for tRNA modification activity in eukaryotes.

   Cryo-EM structure of the fully assembled Elongator complex. · Jaciuk M, Scherf D, et al. · Nucleic Acids Res 2023
   PMID 36617428DOI
   ▸What this evidence cannot show

   Yeast and mouse structures; the human arm of this paper is biochemical characterisation rather than a human structure, so 'the structure of the fully assembled complex' is not a human structure and this entry does not claim one. Abstract read; full text not read. The substrate throughout is tRNA - the paper's framing of Elongator is entirely as a wobble-uridine modification enzyme, with no histone activity discussed in the abstract.

   ▸Evidence that argues against this (1)

   • A structural paper's framing is not evidence against an activity it did not assay. But it is worth noting that the two 2023-2024 structural papers on this complex treat it as a tRNA enzyme without qualification, which is a measure of where the field has moved rather than an argument. Winkler GS et al. 2002
8. E9established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.paper

   Rare germline loss-of-function variants in ELP1 occur in 14% of paediatric Sonic-Hedgehog medulloblastoma with universal biallelic inactivation through somatic 9q loss, and the tumours show a destabilised Elongator complex, loss of Elongator-dependent tRNA modifications, codon-dependent translational reprogramming and induction of the unfolded-protein response.

   Germline Elongator mutations in Sonic Hedgehog medulloblastoma. · Waszak SM, Robinson GW, et al. · Nature 2020
   PMID 32296180DOI
   ▸What this evidence cannot show

   Cited in THIS entry as the second of the three lineage results and for the comparison in E2; the full treatment lives in gene-elp1. Brain tumour, not leukaemia, cooperating with SHH-pathway activation.

   ▸Evidence that argues against this (1)

   • ELP1 and not ELP5, and a predisposition rather than a dependency - so it establishes that Elongator loss can drive a paediatric cancer and says nothing about whether ELP5 loss would. Close P et al. 2012
9. 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
10. 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
11. 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
12. E3weak confidence 2 of 5: Preliminary, small, indirect, or not yet peer reviewed.dataset

    ELP5 shows no KMT2A-selective dependency in this project's own DepMap scan: mean Chronos -1.1965 in 11 KMT2A-rearranged lines against -1.1088 in 43 other leukaemia lines, difference -0.0878, at a pan-essentiality of -1.2094 across 1208 lines and selectivity rank 1473 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 -0.0878 at a pan-essentiality of -1.209 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
    • ELP5 is the DEEPEST of the six subunits at -1.209 (against ELP1 -1.022, ELP6 -0.981, ELP3 -0.965, ELP2 -0.627, ELP4 -0.459) and is the member supplying the best_rank of 1,473 in this project's own analyses/complex-level-coherence scoring of the Elongator holoenzyme (IntAct CPX-1949, median coherence 0.5571, median selectivity rank 7,272). That is a fact about essentiality and NOT about KMT2A: the arm-to-arm difference is -0.088 and the gene is depleted in nearly every line, so there is no dynamic range in which selectivity could appear. The complex-coherence figure was NOT re-run this cycle and scripts/check-analysis-staleness.py should be consulted before it is quoted as live. Oncofusion knowledge-graph project 2026

• binds →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

  ELP5 is required for OPTIMAL BINDING OF ELP3 TO ELP4 and directly connects them; both sit in the accessory ELP4/5/6 hetero-hexamer

• binds →ELP3 - 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

  ELP5 directly connects ELP3 to ELP4 and is required for Elongator integrity

• part of →ELP6 (TMEM103/C3orf75) - an Elongator subunit named after a membrane protein it is not, whose entire localisation record comes from a Drosophila paper its own symbol cannot retrieve

  both in the accessory ELP4/5/6 hetero-hexamer; identified together as human ELP5 and ELP6 in one 2012 paper

• related to →TP53 - named in 84 entries of this graph, absent from the index genome study of the disease, and four different things depending on when you look

  ORPHAN CONVERGENCE, not a mechanism: DERP6/ELP5 overexpression activated p53 transcriptional activity in a 2006 reporter assay, and loss of Elp3 activates a p53 checkpoint in mouse marrow - opposite signs, no paper cites both

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

  BOUNDED ABSENCE, and small-literature: 0 records against controls of 104/30/218, but ELP5 total literature is 22 records and its IntAct bait has only 13 curated partners

• tests →Hypothesis: transfer-RNA and ribosome biology is a genuinely empty cell in KMT2A-rearranged leukemia, and translational capacity may be the unmeasured dependency

  ELP5 is the assembly bridge of the tRNA wobble-modification complex and the deepest DepMap dependency of the six subunits

• ← part ofELP6 (TMEM103/C3orf75) - an Elongator subunit named after a membrane protein it is not, whose entire localisation record comes from a Drosophila paper its own symbol cannot retrieve

  identified together as human ELP5 and ELP6 in one 2012 paper; both depletions phenocopy Elongator loss in melanoma cells