SKIC8 (formerly WDR61) — the last PAF1C subunit, and a gene-symbol trap worth recording
also called SKIC8 · WDR61 · SKI8 · Ski8 homolog · REC14
SKIC8 is the sixth and smallest part of PAF1C, the complex the KMT2A fusion grabs with a piece it still has. It used to be called WDR61, and looking it up under the old name returns nothing, which is how identifiers quietly go wrong.
The same thing, for a scientist
SKIC8 (Q9GZS3, 305 aa) is a WD40-repeat protein and the sixth subunit of PAF1C, also a component of the SKI complex. It completes the PAF1C roster in this graph alongside PAF1, CTR9, CDC73, LEO1 and RTF1. The PAF1C-KMT2A interaction is mapped to sequences flanking the CxxC domain, which is retained in every clinical KMT2A fusion, so PAF1C is a genuine fusion-interactome complex — but no work attributes the contact to SKIC8 specifically. Dependency: mean gene effect **-0.746** across 1,208 lines with **81.0%** of lines depleted and a KMT2A-selectivity of **-0.016**, i.e. broadly required and entirely non-selective. **The entry also records an identifier trap:** a UniProt query for `gene_exact:WDR61 AND organism_id:9606 AND reviewed:true` returns no entry whose primary gene name is WDR61, because HGNC renamed the gene **SKIC8**. A lookup that accepted the first returned accession without reading back the primary gene name would have produced a silent mismatch of exactly the kind this project has logged six times.
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.
I have never read one of these pictures before
A protein is one long chain of amino acids that folds up. The ribbon traces that chain from one end to the other; it is not a wire, it is a simplification of where the backbone runs. Drag to rotate, scroll to zoom.
Domains are the stretches of chain that do a particular job, and they are what the coloured blocks above the picture mark out. Click one and the view flies to it. In this project the important question about any domain is usually whether the fusion still has it — the labels say lost where it does not.
Anything in yellow sticks is a bound small molecule, which is usually the drug.
The identifier trap, stated first because it is the transferable part
This project's standing rule is to fetch an accession and read back its primary gene name rather than trusting a search that looks exact. Resolving this protein exercised the rule in a new direction.
Querying UniProt for gene_exact:WDR61 AND organism_id:9606 AND reviewed:true returns Q9GZS3, whose primary gene name is SKIC8 — not WDR61. WDR61 is now a synonym. The protein is the right one; the symbol is stale 2.
That is a different failure mode from the TCF3/TCF7L1 trap already on record. There the query returned the wrong protein under a synonym match. Here the query returns the right protein under an outdated primary symbol, so a check that only compared 'did I get a hit' would pass while a check that compared 'is the primary gene name what I asked for' would fail and need a human decision. Both checks are necessary; neither alone is sufficient. Any entry in this graph that stores gene_symbol: "WDR61" will fail verify-accessions.py, and this entry stores SKIC8 with WDR61 as an alias.
PAF1C membership and the fusion
SKIC8/WDR61 is a WD40-repeat protein present in both PAF1C and the SKI complex. Its inclusion here completes the PAF1C roster in this graph.
The complex-level claim is strong: MLL/KMT2A interacts directly with PAF1C through sequences flanking the CxxC domain, PAF1C augments MLL- and MLL-AF9-mediated Hoxa9 activation, knockdown disrupts fusion-mediated activation and recruitment, and MLL deletions that abolish the PAF1C interaction eliminate MLL-AF9 immortalisation 1. Because the CxxC region is retained in every clinical fusion, PAF1C is a bona fide member of the KMT2A fusion interactome — one of the few in this beat.
The subunit-level claim is weak: nothing attributes the KMT2A contact to SKIC8. Method: as for RTF1 — complex-level interaction mapping and functional genetics 1. Shown for: wild-type KMT2A and MLL-AF9. Which part of the fusion: the retained KMT2A N-terminus.
Dependency: -0.746 mean, 81.0% of lines depleted, KMT2A-selectivity -0.016 2. Broadly required, no window.
| uniprot | Q9GZS3 |
|---|---|
| gene symbol | SKIC8 |
| length AA | 305 |
| protein name | Superkiller complex protein 8 (WD repeat-containing protein 61) |
| alphafold ID | AF-Q9GZS3-F1 |
| accession resolution | UniProt query gene_exact:WDR61 AND organism_id:9606 AND reviewed:true returned Q9GZS3 whose PRIMARY gene name is SKIC8; WDR61 is now a synonym. Length 305 confirmed. Stored under the primary symbol SKIC8 so that verify-accessions.py passes. |
| former symbol | WDR61 |
| identifier trap | A lookup that accepted the first hit of a WDR61 query without reading back the primary gene name would have stored a stale symbol and failed accession verification silently. This is the second distinct failure mode logged in this project: the first (TCF3 returning TCF7L1) was a wrong protein under a synonym; this one is the right protein under an outdated symbol. |
| interaction evidence class | complex-level interaction mapping and functional genetics; no subunit-level attribution |
| shown for fusion | yes at complex level, for MLL-AF9 |
| druggability | Not a target. A WD40 protein required by 81% of lines with no selectivity. |
| subnuclear localization | NONE ASSIGNED AS A COMPARTMENT - a bounded absence - BUT THERE IS A CHROMATIN ADDRESS, AND IT IS CONDITIONAL ON PAF1C. ChIP shows hSKI associating with transcriptionally active genes only when hPAF is present [E_q91_skic8_loc2]. That is a genomic address rather than a nuclear body, and it is recorded here in the same way SMARCD1's enhancer occupancy is: as a position on DNA, not a place in the nucleus. No nucleolar, speckle, PML-body or lamina assignment exists for SKIC8 under any of its three names. |
| localization shown for fusion | NO for localisation, in any fusion, in any lineage. The fusion link is at complex level only: PAF1C interacts with sequences flanking the KMT2A CxxC domain, which every clinical fusion retains, and the PAF complex synergises with MLL fusion proteins at HOX loci (this entry's E1, PMID 20541477) - work that attributes nothing to SKIC8 specifically and reports no compartment. Bounded and it is a clean demonstration of the retired-symbol trap: SKIC8[tiab] AND MLL[tiab] = 0, WDR61[tiab] AND MLL[tiab] = 0 AND SKI8[tiab] AND MLL[tiab] = 0, i.e. all three spellings return zero while the entry's own founding citation is an MLL-fusion paper - because that paper names the COMPLEX and not the subunit [E_q91_skic8_loc4]. |
complexes
[ "PAF1C (polymerase-associated factor complex)", "SKI complex" ]
paf1c subunits in graph
[ "gene-paf1", "gene-ctr9", "gene-cdc73", "gene-leo1", "gene-rtf1", "gene-skic8 (this entry)" ]
contact on kmt2a
{
"kmt2a_region": "sequences flanking the CxxC domain (complex-level claim)",
"retained_in_fusion": true,
"attributed_to_skic8_specifically": false
}essentiality
{
"depmap_common_essential": false,
"chronos_mean": -0.7458,
"n_lines": 1208,
"fraction_lines_depleted": 0.8104,
"chronos_mean_kmt2a_rearranged": -0.8312,
"chronos_mean_other_leukemia": -0.8149,
"kmt2a_selectivity_difference": -0.0163,
"n_kmt2a_rearranged_lines": 11,
"n_other_leukemia_lines": 43,
"benchmark_men1_difference": -0.8656
}localization
{
"CONSTITUTIVE": "BOTH NUCLEUS AND CYTOPLASM, and for this protein that is a statement about which of its TWO complexes it is in rather than a vague dual localisation. UniProt Q9GZS3 (fetched live 2026-09-21) gives 'Nucleus' on ECO:0000269 PubMed:16024656 and PubMed:18445686, and 'Cytoplasm' on ECO:0000269 PubMed:18445686 plus ECO:0000305 PubMed:16024656 [E_q91_skic8_loc1].",
"THE_TWO_COMPLEXES_SIT_IN_DIFFERENT_PLACES_AND_THE_HUMAN_CASE_DIFFERS_FROM_YEAST": "hSki8/SKIC8 is a subunit of BOTH the human PAF complex and the human SKI complex. The founding human paper states the split explicitly and flags the species difference: the YEAST SKI complex is CYTOPLASMIC and with the exosome mediates 3'-5' mRNA degradation, but the HUMAN SKI COMPLEX LOCALIZES TO BOTH NUCLEUS AND CYTOPLASM - and hSKI associates with TRANSCRIPTIONALLY ACTIVE GENES in a manner DEPENDENT ON THE PRESENCE OF hPAF [E_q91_skic8_loc2]. So the nuclear pool of SKIC8 is, at least in part, PAF1C-dependent, which is the pool that matters to this graph.",
"no_induced_relocalisation_recorded": "None in UniProt and none retrieved."
}cell type
{
"measured_in": "Human cell lines in the hPAF/hSKI characterisation [E_q91_skic8_loc2]; the second UniProt source is a proteomic survey of nuclear microtubule-binding proteins in HeLa-type cells [E_q91_skic8_loc3].",
"haematopoietic": "NONE. SKIC8 has never been localised in a haematopoietic cell, and the PAF1C-KMT2A-fusion work that puts it in this graph (this entry's E1, PMID 20541477) does not resolve individual subunits.",
"expression_note": "DepMap gives a mean gene effect of -0.746 with 81.0% of lines depleted and a KMT2A-selectivity of -0.016 (this entry's existing data) - broadly required, entirely non-selective, so nothing about cell type is inferable from dependency either."
}cell state
{
"not_recorded": "No cell-cycle, damage or differentiation-dependent redistribution has been reported.",
"THE_STATE_THAT_IS_ACTUALLY_DEFINED_HERE_IS_COMPLEX_OCCUPANCY": "SKIC8's compartment is a function of which complex holds it, and RNAi against hSki8 reduces the cellular levels of the other hPAF subunits and of H3K4me1/me3 and H3K79me2 [E_q91_skic8_loc2] - so the subunit cannot be removed without dismantling the complex whose localisation defines it. Any experiment that asks 'where is SKIC8 when PAF1C is gone' destroys its own readout."
}localization bounded absence
{
"date": "2026-09-22",
"tool": "NCBI esearch db=pubmed",
"run_by": "Q91",
"queries": [
{
"query": "SKIC8[tiab]",
"querytranslation": "\"SKIC8\"[Title/Abstract]",
"count": 2,
"role": "the CURRENT HGNC symbol"
},
{
"query": "WDR61[tiab]",
"querytranslation": "\"WDR61\"[Title/Abstract]",
"count": 9,
"role": "the previous official symbol"
},
{
"query": "SKI8[tiab]",
"querytranslation": "\"SKI8\"[Title/Abstract]",
"count": 43,
"role": "the complex-derived name the field actually uses"
},
{
"query": "WDR61[tiab] AND (nuclear[tiab] OR cytoplasm[tiab] OR localization[tiab])",
"querytranslation": "\"WDR61\"[Title/Abstract] AND (\"nuclear\"[Title/Abstract] OR \"cytoplasm\"[Title/Abstract] OR \"localization\"[Title/Abstract])",
"count": 0
},
{
"query": "SKIC8[tiab] AND MLL[tiab]",
"querytranslation": "\"SKIC8\"[Title/Abstract] AND \"MLL\"[Title/Abstract]",
"count": 0
},
{
"query": "WDR61[tiab] AND MLL[tiab]",
"querytranslation": "\"WDR61\"[Title/Abstract] AND \"MLL\"[Title/Abstract]",
"count": 0
},
{
"query": "SKI8[tiab] AND MLL[tiab]",
"querytranslation": "\"SKI8\"[Title/Abstract] AND \"MLL\"[Title/Abstract]",
"count": 0
}
],
"reading": "THE SYMBOL RATIO IS THE RESULT: 2 : 9 : 43 across SKIC8, WDR61 and SKI8. A beat keyed to the current HGNC symbol reaches 4.7% of this protein's literature. The dispatch brief predicted exactly this for SKIC8 and it is confirmed, with the twist that the retired OFFICIAL symbol WDR61 is not the productive one either - the complex-derived trivial name SKI8 is. Titles and abstracts only (rule 80); REC14 and hSki8 were not run as separate operands.",
"absence_class": "never-measured"
}- SKIC8 sits in two unrelated complexes, so any agent against it would hit RNA surveillance as well as transcription elongation.
- Required in 81% of cell lines with no KMT2A selectivity: no therapeutic window.
- Does SKIC8 participate in the KMT2A contact at all, or is it purely structural within PAF1C?
- SKIC8 is shared between PAF1C and the SKI complex. Does knocking it down perturb RNA surveillance in a way that confounds any PAF1C-directed experiment?
- How many other gene symbols stored in this graph are stale rather than wrong? A sweep comparing every stored gene_symbol against the current HGNC primary symbol would take minutes and has not been run.
- E1established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.paper
MLL interacts directly with the polymerase-associated factor complex through sequences flanking the CxxC domain; PAFc augments MLL- and MLL-AF9-mediated transcriptional activation of Hoxa9; PAFc knockdown disrupts MLL fusion protein-mediated activation and MLL recruitment to target loci; and MLL deletions abolishing PAFc interaction eliminate MLL-AF9-mediated immortalisation.
The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. · Muntean AG, Tan J, Sitwala K, Huang Y, Bronstein J, Connelly JA, Basrur V, Elenitoba-Johnson KSJ, Hess JL · Cancer Cell 2010What this evidence cannot show
Abstract read in full; not full text. The claim is at complex level; the abstract names no individual PAF1C subunit as the KMT2A contact, and SKIC8/WDR61 in particular is not mentioned. The fusion tested is MLL-AF9 in murine immortalisation assays, not KMT2A::AFF1. INTERACTION PROVENANCE (Q76, 2026-09-21, live IntAct REST), which puts a number on 'no work attributes the contact to SKIC8 specifically': all three IntAct records for the KMT2A-SKIC8 pair are psi-mi:MI:1060 spoke-expanded and typed MI:0914 association, and all three come from this same publication (PMID 20541477) - so the pair rests on one experiment, spoke-expanded, and no PDB entry contains both Q9GZS3 and Q03164. Within PAF1C the gradient is visible: KMT2A-PAF1, KMT2A-CTR9 and KMT2A-CDC73 each have at least one record that is NOT spoke-expanded, while KMT2A-SKIC8 and KMT2A-LEO1 have none. The spoke rows remain a real observation that SKIC8 was in the pulldown; what they cannot support is a SKIC8-KMT2A contact. See ana-two-thirds-of-the-curated-interactome-is-a-row-nobody-observed.
Evidence that argues against this (2)
- The entry's framing of a settled 'PAF1C roster in this graph alongside PAF1, CTR9, CDC73, LEO1 and RTF1' is not settled. Cao et al. report that Rtf1 'is not stably associated with the PAF1C in most species except Saccharomyces cerevisiae', that human Rtf1 functions as an elongation factor independently of PAF1C, and that PAF1C recruitment at the genes tested was Rtf1-independent. A six-subunit roster that includes RTF1 imports a yeast composition into a human complex. The correct statement for this graph is a five-subunit human core (PAF1, CTR9, CDC73, LEO1, SKIC8) plus RTF1 as a disputed, sub-stoichiometric associate. Read: abstract in full, not full text. Cao QF et al. 2015
- The therapeutic sign of a PAF1C-directed manoeuvre is also unsettled, which bears on why SKIC8's -0.016 selectivity matters less than it looks. Chen et al. show PAF1 reduction releases paused Pol II into gene bodies at thousands of genes and raises transcript levels via super-elongation-complex recruitment; Yu et al., four months later in Science, report PAF1 as required for paused Pol II release and for CDK12 recruitment. Until that is resolved, a PAF1C subunit cannot be scored as a handle on the fusion in either direction. Read: abstracts in full, not full text. Chen FX et al. 2015
- E2strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.database
A UniProt query for gene_exact:WDR61 AND organism_id:9606 AND reviewed:true returns Q9GZS3 whose primary gene name is SKIC8, not WDR61; the protein is 305 aa. SKIC8 has DepMap mean gene effect -0.7458 across 1,208 lines with 81.0% of lines depleted, mean -0.8312 in 11 KMT2A-rearranged leukemia lines against -0.8149 in 43 other leukemia lines (difference -0.016).
UniProtKB REST API (gene_exact query with primary gene name read back) and DepMap CRISPR (Chronos) gene effect via the Open Targets Platform GraphQL API, with KMT2A-rearrangement status from Cellosaurus; resolved for this beat on 2026-09-18 · UniProt Consortium; Broad Institute DepMap; Cellosaurus; Open Targets Platform; analysis run by this project · Databases and derived analysis 2026What this evidence cannot show
DepMap release version not stated by the API. The symbol change is recorded as observed on 2026-09-18; nomenclature can change again, and the durable identifier is the accession Q9GZS3, not either symbol.
Evidence that argues against this (1)
- The identifier-trap lesson is sound and the subunit-assignment lesson should sit beside it: co-purification alone does not establish stoichiometric membership. van Nuland et al. used label-free quantitative mass spectrometry on the human SET1/MLL complexes specifically to separate 'known and novel, unique and shared interactors' and to determine their stoichiometry, and in doing so reassigned DPY30 as a genuine NURF subunit as well as a COMPASS one and identified BOD1 as a SET1B-versus-SET1A discriminator. No equivalent quantification exists for the human PAF1C roster this entry completes, so subunit status here is qualitative. Read: abstract in full, not full text. van Nuland R et al. 2013
- E_q91_skic8_loc1established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.database
UniProtKB Q9GZS3 (SKI8_HUMAN, primary gene SKIC8, 305 aa, read back live 2026-09-21) carries TWO subcellular location values: 'Nucleus' on ECO:0000269 PubMed:16024656 and PubMed:18445686, and 'Cytoplasm' on ECO:0000269 PubMed:18445686 plus ECO:0000305 PubMed:16024656. There is no location note and no complex-scoped comment, so the database does not record that the two compartments correspond to two different complexes. Note also that the UniProt ENTRY NAME is still SKI8_HUMAN while the primary gene name is SKIC8 - a third spelling inside one record.
UniProtKB Q9GZS3 SUBCELLULAR LOCATION comments, evidence codes and feature table, fetched live 2026-09-21 (nucleus and cytoplasm, and an entry name that is a third spelling of the symbol) · UniProt Consortium · UniProtKB 2026What this evidence cannot show
One of the two cited experimental papers is not about this protein at all (see E_q91_skic8_loc3). The cytoplasm call from PubMed:16024656 is correctly graded ECO:0000305 - a curator inference - because that paper's statement about cytoplasmic SKI is about the YEAST complex.
Evidence that argues against this (1)
- The record's own grading is the evidence against reading 'Cytoplasm' as firmly as 'Nucleus', and it is easy to miss. For the same source paper UniProt used ECO:0000269 for the nucleus and ECO:0000305 for the cytoplasm - the curator saw a human nuclear observation and INFERRED the cytoplasmic one, presumably from the yeast SKI complex the paper contrasts against. This is rule 91 item 4 in action, and it means that a filter keeping only ECO:0000269 would keep both compartments for this protein (because the second paper supplies a coded cytoplasm too) while silently discarding the one distinction that carries information. Zhu B et al. 2005
- E_q91_skic8_loc2strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper
The founding human paper is explicit about the compartment and about the species difference: hPAF shares four subunits with yeast PAF (hCtr9, hPaf1, hLeo1, hCdc73) but contains a novel higher-eukaryote-specific subunit, hSki8, which is ALSO a component of the human SKI complex; the YEAST SKI complex is CYTOPLASMIC and mediates 3'-5' mRNA degradation with the exosome, but THE HUMAN SKI COMPLEX LOCALIZES TO BOTH NUCLEUS AND CYTOPLASM. Immunoprecipitation shows hPAF and hSKI interact, and ChIP shows hSKI associating with TRANSCRIPTIONALLY ACTIVE GENES DEPENDENT ON THE PRESENCE OF hPAF. RNAi against hSki8 or hCtr9 reduces the cellular levels of the other hPAF subunits and of mono- and trimethylated H3K4 and dimethylated H3K79.
The human PAF complex coordinates transcription with events downstream of RNA synthesis. · Zhu B, Mandal SS, Pham AD, Zheng Y et al. · Genes Dev 2005What this evidence cannot show
2005, human cell lines, not haematopoietic and no fusion. 'Localizes to both nucleus and cytoplasm' is a statement about the hSKI COMPLEX rather than about hSki8 in isolation, and the paper does not partition the protein quantitatively between its two complexes. Read from the abstract.
Evidence that argues against this (1)
- This is the one place where transferring the yeast result would have inverted the answer, and it argues against a habit this project relies on elsewhere. Yeast Ski8 sits in a cytoplasmic complex; the obvious inference for a conserved WD40 subunit is cytoplasmic, and it is wrong for human - the human SKI complex is in both compartments and is recruited to active genes by PAF1C. Note the contrast with SMC3 in this same tranche, whose entire human compartment record is an ECO:0000250 transfer from mouse and is probably fine. Orthologue transfer of a compartment is safe or unsafe depending on the protein, and nothing in the annotation tells a reader which case they are in. UniProt Consortium 2026
- E_q91_skic8_loc3moderate confidence 3 of 5: One strong study, or several smaller consistent ones.paper
RULE-91 INSTANCE. UniProt's second experimental citation for both of SKIC8's compartments, PubMed:18445686, is a paper about a DIFFERENT PROTEIN: 'EML3 is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase'. It used a proteomic approach to identify mitotic microtubule-binding proteins that localise to the nucleus in interphase and 'revealed 50 poorly characterised human gene products', then pursued EML3 by immunofluorescence. SKIC8/WDR61 is one of the unnamed entries in that list of fifty, and the localisation attributed to it is therefore membership of a proteomic fraction rather than an observation of the protein.
EML3 is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. · Tegha-Dunghu J, Neumann B, Reber S, Krause R et al. · J Cell Sci 2008What this evidence cannot show
Read from the abstract, which names only EML3 among the fifty; the supplementary list was not retrieved, so it cannot be confirmed from here which fraction SKIC8 appeared in or at what confidence. That uncertainty is the point - the annotation is only as good as a table nobody has opened.
Evidence that argues against this (1)
- In fairness the inference is not baseless: the fraction was defined as proteins that ARE nuclear in interphase, so membership carries some localisation information, which makes this weaker than tranche 3's BICRA case where the source contained no microscopy at all and no localisation-defined fraction. The objection that stands is different and sharper. The fraction was selected for MITOTIC MICROTUBULE BINDING, and if SKIC8 is in it then SKIC8 is a candidate microtubule-associated protein - an implication with no follow-up anywhere, which nobody has tested, and which is entirely absent from this entry, from PAF1C biology and from the SKI complex literature. The annotation may be sound and its provenance is still telling the reader something nobody has pursued. Zhu B et al. 2005
- E_q91_skic8_loc4moderate confidence 3 of 5: One strong study, or several smaller consistent ones.database
Counted absence and a measured symbol ratio, 2026-09-22, querytranslation read back on every line. Total literature by spelling: SKIC8[tiab] = 2, WDR61[tiab] = 9, SKI8[tiab] = 43. Against the disease: SKIC8[tiab] AND MLL[tiab] = 0, WDR61[tiab] AND MLL[tiab] = 0, SKI8[tiab] AND MLL[tiab] = 0. Localisation under the retired official symbol: WDR61[tiab] AND (nuclear OR cytoplasm OR localization)[tiab] = 0.
Three-spelling symbol ratio and counted absence for SKIC8/WDR61/SKI8 against MLL, querytranslation recorded, run 2026-09-22 · NCBI E-utilities esearch (db=pubmed), run by Q91 · PubMed E-utilities 2026What this evidence cannot show
Bounded by titles and abstracts (rule 80). Three spellings were run; hSki8, Ski8p and REC14 were not, and SKI8 as a bare token is short enough to warrant title-checking before its 43 are treated as on-topic, which was not done - the 43 is used here only as a denominator for the ratio, not as a claim about content.
Evidence that argues against this (1)
- The three zeros against MLL would read as a clean absence and they are an artefact of the same kind rule 64 documents for FACT and SSRP1. This entry's own founding citation, PMID 20541477, is titled 'The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis' - an MLL-fusion paper about the complex SKIC8 belongs to, invisible to all three subunit spellings because it names the complex. So the absence that survives is narrow (nobody has attributed anything to SKIC8 specifically in this disease) and the absence a symbol query appears to show (no link between this protein and MLL) is false. Muntean AG et al. 2010
PAF1C is the hypothesis's second retained-fragment handle, but its human roster and the sign of its effect on elongation are both unsettled
- ← related toRTF1 — the PAF1C subunit the graph was missing, on a complex that does bind the retained KMT2A fragment
the two PAF1C subunits the graph was missing before this cycle
sixth PAF1C subunit (formerly WDR61)
same complex
PAF1C-KMT2A contact at the retained CxxC-flanking region; not attributed to SKIC8 specifically
SKIC8's NUCLEAR pool is PAF1C-associated and hSKI's chromatin occupancy at active genes is hPAF-DEPENDENT (PMID 16024656) - the compartment follows the complex (Q91 2026-09-22)
RULE-91 INSTANCE: UniProt's second experimental citation for both SKIC8 compartments is an EML3 paper in which SKIC8 is one of 50 unnamed proteomic hits; and the yeast-to-human transfer would have called it cytoplasmic, which is wrong (Q91 2026-09-22)