ACTR8

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0003729 mRNA binding	IBA GO_REF:0000033	MARK AS OVER ANNOTATED	Summary: A single yeast RIP-chip result propagated as a molecular function to 87 ARP8 orthologues across all eukaryotes. The donor annotation is genuine, but the assay cannot separate mRNA binding from the general single-stranded nucleic-acid binding that human ARP8 is actually characterised for, and the binding element it depends on differs in length between yeast and human. Reason: Resolving the donors and then querying their own evidence shows this row is not the family-level guess it first appears to be, and the obvious dismissal is wrong. The committed PAINT file records GO:0003729 as IBD from SGD:S000005667 alone, added 2025-08-05 - but a single donor is not by itself the objection, and claiming otherwise would contradict this review's own GO:0006302 row. Donor counts at PTN000234048 are GO:0031011 four, GO:0006355 two, and GO:0003729 and GO:0006302 one each - and GO:0006302 is accepted here. What separates them is target-side evidence: human ARP8 has direct experimental data for a role in double-strand break repair and none whatever for RNA binding. That is the criterion this review applies throughout. The donor, Saccharomyces cerevisiae ARP8 (Q12386, Swiss-Prot), does carry its own IDA, from PMID:20844764, and yeast ARP8 is in that paper's confirmed set rather than among its unvalidated candidates: it appears in the table of novel RBPs confirmed by IP-microarray, with 231 targets at FDR <= 0.01 % - the Methods define the cut-off as a SAM-calculated false discovery rate less than or equal to 0.01 %, so it is 100-fold stricter than a bare 0.01 would suggest - at a point where only 12 of 35 candidates survived validation. So SOURCE_EVIDENCE_WEAK would be factually contradicted by my own analysis; the source annotation is sound. The propagation is what fails, on three grounds. (1) One donor and one study support a molecular-function term that now sits on all 87 members of the node, spanning plants, fungi, metazoa, Giardia and Paramecium, and no member outside S. cerevisiae has ever been assayed for it. (2) The screen design cannot distinguish the ligand class: the primary assay bound RNA samples to protein microarrays, with no DNA competitor anywhere in the design, so for a protein whose nucleic-acid-binding element is a basic disordered N-terminal extension and whose demonstrated preference is for single-stranded nucleic acid, 'binds mRNA' and 'binds single-stranded polyanion' are not separable by this experiment. Human ARP8's characterised nucleic-acid ligands are ssDNA (preferentially) and dsDNA; no one has assayed human ARP8 with RNA at all. (3) The binding element is not conserved in size between donor and target - but this ground is weaker than it first looks, and is reported at its true strength. Reading the sentence to the end of its qualifying clause, PMID:22977180 says the N-terminal extension is rather short in human Arp8 compared to yeast Arp8 but still comprises 46 mostly charged residues. So the human protein retains a substantial basic extension; the size asymmetry (yeast 881 aa against human 624 aa, much of the difference in this region) makes the transfer less safe without making it impossible. Grounds (1) and (2) carry the argument; (3) only supports it. MARK_AS_OVER_ANNOTATED rather than REMOVE, deliberately. REMOVE needs a positive argument and I have none: there is no human negative, only an absence of human RNA data, and an absence is not a finding. The right classification is PROPAGATION_BAD - the source annotation is sound but the term should not propagate to this target - which is what this reason argues, and it is why SOURCE_EVIDENCE_WEAK is deliberately absent from failure_modes. GRANULARITY_MISMATCH is used in the second sense its definition allows, child term overstates specificity: the donor's own term names a ligand class its assay did not discriminate. It is not used in the parent-true-but-uninformative sense, and FUNCTIONAL_DIVERGENCE is deliberately not claimed, because a change of ligand class in the human protein has not been demonstrated - only that its characterised ligand is a different one. Recommendation for PAINT: restrict GO:0003729 to the S. cerevisiae leaf until an orthologue outside yeast has been assayed with RNA against a DNA competitor. Propagation Review Root cause: PROPAGATION BAD Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000234048 · PANTHER ARP8 orthogroup node (87 gene products) UNRESOLVED PANTHER internal tree node, not a protein. Census via QuickGO withFrom (numberOfHits 348, all fetched): 87 gene products, every one an ARP8 orthologue (ARP8/ACTR8/actr8/arp8/arp-8/arpG/plant ARP9) across plants, fungi, metazoa, Giardia and Paramecium; zero conventional actins. All 87 carry exactly the same 4 terms, so this is an ARP8-specific orthogroup node. SGD:S000005667 · S. cerevisiae ARP8 (Q12386) SUPPORTS TRANSFER Q12386 ARP8_YEAST, Saccharomyces cerevisiae ARP8, Swiss-Prot reviewed, 881 aa. True ARP8 orthologue, not a paralog. Supporting Evidence: PMID:20844764 Novel RBPs identified in the protein microarray experiments and confirmed by IP-microarray experiments. PMID:20844764 Of 35 putative novel RBPs identified by either or both of these methods, 12, including 75% of the eight most highly-ranked candidates, reproducibly associated with specific cellular RNAs. PMID:20844764 We describe here a proteome-wide approach to identify RNA-protein interactions based on in vitro binding of RNA samples to yeast protein microarrays that represent over 80% of the yeast proteome. PMID:25299602 we showed that recombinant human Arp8 binds to DNAs, and preferentially binds to single-stranded DNA PMID:25299602 The N-terminal extension of the human Arp8 is abundant in basic amino acids. PMID:22977180 It is rather short in human Arp8 compared to yeast Arp8, but still comprises 46 mostly charged residues file:interpro/panther/PTHR11937/PTHR11937-paint.tsv PTHR11937 PTN000234048 GO:0003729 F IBD false SGD:S000005667
GO:0006355 regulation of DNA-templated transcription	IBA GO_REF:0000033	ACCEPT	Summary: Self-referential IBA recording a PAINT curator's judgement that transcriptional regulation is a core ARP8 function, corroborated by a Drosophila Arp8 IMP. The direction-neutral parent is the correct term because the INO80 complex both activates and represses. Reason: The WITH/FROM list contains UniProtKB:Q9H981 itself, so this is a self-referential IBA and NO_FAILURE_CORE applies: a curator judged the function core for ACTR8 rather than inferring it from elsewhere. The non-self donor, Drosophila Arp8 (Q9VX09, Swiss-Prot), carries its own IMP to exactly this term from PMID:16618800, so ortholog-strength support is available and does not sit above the donor's own granularity. No specificity upgrade is proposed, and this is a considered refusal rather than an omission. ACTR8 does carry its own IMP to the child GO:0045893 (positive regulation), which would normally invite a downward MODIFY. But the complex works in both directions: it activates oncogenic transcription at enhancers in NSCLC and it represses p21 through p53. GRANULARITY_MISMATCH requires the donors to agree, and here the target's own data disagree with itself on sign, so the direction-neutral parent is the genuine least common ancestor and the signed child is the narrower, context-specific statement. Accepted as core; the signed child row is kept non-core. Propagation Review Root cause: NO FAILURE CORE Sources checked: FB:FBgn0030877 · D. melanogaster Arp8 (Q9VX09) SUPPORTS TRANSFER Q9VX09 ARP8_DROME, Drosophila melanogaster Arp8, Swiss-Prot reviewed, 607 aa. True ARP8 orthologue. PANTHER:PTN000234048 · PANTHER ARP8 orthogroup node (87 gene products) UNRESOLVED PANTHER internal tree node, not a protein. Census via QuickGO withFrom (numberOfHits 348, all fetched): 87 gene products, every one an ARP8 orthologue (ARP8/ACTR8/actr8/arp8/arp-8/arpG/plant ARP9) across plants, fungi, metazoa, Giardia and Paramecium; zero conventional actins. All 87 carry exactly the same 4 terms, so this is an ARP8-specific orthogroup node. UniProtKB:Q9H981 · human ACTR8 (self) SUPPORTS TRANSFER Self-referential: the WITH/FROM list contains ACTR8 itself, so this records a PAINT curator judging the function core for this gene rather than inferring it. Supporting Evidence: PMID:27641337 It occupies enhancer regions near lung cancer-associated genes, and its occupancy correlates with increased genome accessibility and enhanced expression of downstream genes. PMID:26340092 we first demonstrate that INO80 complex negatively regulates the p21Waf1/Cip1 (p21) expression in a p53-mediated mechanism file:interpro/panther/PTHR11937/PTHR11937-paint.tsv PTHR11937 PTN000234048 GO:0006355 P IBD false UniProtKB:Q9H981\|FB:FBgn0030877
GO:0031011 Ino80 complex	IBA GO_REF:0000033	ACCEPT	Summary: The best-supported row in the set: four independent experimental donors plus ACTR8 itself, and the target additionally has its own IDA to the same term. Reason: Every non-node donor resolves to a genuine ARP8 orthologue and every one carries its own experimental evidence for this exact term, checked per accession in QuickGO: yeast ARP8 IPI (PMID:10952318, PMID:24034245), Drosophila Arp8 IDA and IPI (PMID:16618800), S. pombe arp8 IDA (PMID:19040720) and IPI (PMID:19933844). The list also contains UniProtKB:Q9H981, making it partly self-referential, and ACTR8 independently carries two IDA rows to GO:0031011 in this same GOA snapshot. The propagation lands at exactly the term the donors hold, neither above nor below it, so no MODIFY is warranted in either direction. ComplexPortal CPX-846 lists ACTR8 among the 15 participants of the human INO80 chromatin remodeling complex, and the human complex has been purified with ARP8 in it repeatedly. Core. Propagation Review Root cause: NO FAILURE CORE Sources checked: FB:FBgn0030877 · D. melanogaster Arp8 (Q9VX09) SUPPORTS TRANSFER Q9VX09 ARP8_DROME, Drosophila melanogaster Arp8, Swiss-Prot reviewed, 607 aa. True ARP8 orthologue. PANTHER:PTN000234048 · PANTHER ARP8 orthogroup node (87 gene products) UNRESOLVED PANTHER internal tree node, not a protein. Census via QuickGO withFrom (numberOfHits 348, all fetched): 87 gene products, every one an ARP8 orthologue (ARP8/ACTR8/actr8/arp8/arp-8/arpG/plant ARP9) across plants, fungi, metazoa, Giardia and Paramecium; zero conventional actins. All 87 carry exactly the same 4 terms, so this is an ARP8-specific orthogroup node. PomBase:SPAC664.02c · S. pombe arp8 (Q9US07) SUPPORTS TRANSFER Q9US07 ARP8_SCHPO, Schizosaccharomyces pombe arp8, Swiss-Prot reviewed, 662 aa. True ARP8 orthologue. SGD:S000005667 · S. cerevisiae ARP8 (Q12386) SUPPORTS TRANSFER Q12386 ARP8_YEAST, Saccharomyces cerevisiae ARP8, Swiss-Prot reviewed, 881 aa. True ARP8 orthologue, not a paralog. UniProtKB:Q9H981 · human ACTR8 (self) SUPPORTS TRANSFER Self-referential: the WITH/FROM list contains ACTR8 itself, so this records a PAINT curator judging the function core for this gene rather than inferring it. Supporting Evidence: PMID:21303910 the actin-related proteins Arp4 and Arp8, and the GLI-Kruppel family transcription factor YY1 PMID:27257055 The complex comprises one subunit each of an N-terminally truncated Ino80, actin, Arp4, Arp5, Arp8, Ies2 and Ies6, together with a single heterohexamer of the Tip49a and Tip49b proteins. file:interpro/panther/PTHR11937/PTHR11937-paint.tsv PTHR11937 PTN000234048 GO:0031011 C IBD false SGD:S000005667\|FB:FBgn0030877\|UniProtKB:Q9H981\|PomBase:SPAC664.02c
GO:0006302 double-strand break repair	IBA GO_REF:0000033	ACCEPT	Summary: One yeast donor with its own IMP, but the term needs no propagation to stand: human ARP8 is the subunit required for recruiting the mammalian INO80 complex to DNA damage sites, and a human ARP8 knockout is repair-defective. Reason: The single donor, yeast ARP8, carries its own IMP from PMID:23644470, so the source side is sound. More important, this is one of the rows where the human gene has direct evidence that is stronger than the inference: among all the subunits tested by RNAi, only ARP8 was indispensable for recruiting the mammalian complex to damage sites - the qualifier 'tested' is the source's own and is kept rather than rounded up to 'the only subunit' - in contrast to yeast where Nhp10 and Arp4 do that job; a conditional human ARP8 knockout is hypersensitive to aphidicolin and camptothecin; and ARP8's ssDNA preference is the proposed mechanism, since resection generates ssDNA at break ends. ATM- and ATR-dependent phosphorylation of ARP8 then tunes how much INO80 and RAD51 load at breaks, which places ARP8 inside the regulated step rather than merely alongside it. Core, and a good candidate for re-basing on the human experimental evidence. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000234048 · PANTHER ARP8 orthogroup node (87 gene products) UNRESOLVED PANTHER internal tree node, not a protein. Census via QuickGO withFrom (numberOfHits 348, all fetched): 87 gene products, every one an ARP8 orthologue (ARP8/ACTR8/actr8/arp8/arp-8/arpG/plant ARP9) across plants, fungi, metazoa, Giardia and Paramecium; zero conventional actins. All 87 carry exactly the same 4 terms, so this is an ARP8-specific orthogroup node. SGD:S000005667 · S. cerevisiae ARP8 (Q12386) SUPPORTS TRANSFER Q12386 ARP8_YEAST, Saccharomyces cerevisiae ARP8, Swiss-Prot reviewed, 881 aa. True ARP8 orthologue, not a paralog. Supporting Evidence: PMID:20971067 We also found that an actin-related protein, ARP8, is an important subunit that is required for the recruitment of the mammalian INO80 complex to the DNA damage sites PMID:25299602 among all the tested subunits only Arp8 was indispensable for recruiting the INO80 complex to DSB in human cells PMID:25299602 This result suggests that knockout of Arp8 probably impairs DNA repair, which probably takes place via the HR or an HR-like repair process. PMID:25299602 These results suggest that Arp8 binds preferentially to ssDNA and that this property likely contributes to recruiting the INO80 complex to the DSB sites PMID:29759113 The ATM-regulated phosphorylation of ARP8 reduces the excessive loading of INO80 and RAD51 onto the breakpoint cluster region. file:interpro/panther/PTHR11937/PTHR11937-paint.tsv PTHR11937 PTN000234048 GO:0006302 P IBD false SGD:S000005667
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: Correct, and the UniProt statement it derives from is itself experimental. Reason: SL-0191 maps to GO:0005634 and the UniProt SUBCELLULAR LOCATION line it comes from carries ECO:0000269\|PubMed:18163988, so this is an experimentally grounded transfer rather than a prediction. Independently corroborated in this same GOA snapshot by an IDA, an HDA and an HPA nucleoplasm IDA. ARP8 is a constitutively nuclear protein with no reported cytoplasmic pool, which is the point of contrast with the conventional actins in its PANTHER family. The reciprocal check was run, because the merged ACTR10 review had to REMOVE its own GO:0005634 nucleus IBA as a paralog transfer, and a leak that reaches one member of a family can originate in another. ACTR8 is not implicated. ACTR10's nucleus donors are S. cerevisiae ARP9 (a SWI/SNF and RSC subunit), Candida ARP9, mouse Actl7a and an unreviewed Trypanosoma entry, sitting at the deeper node PTN008986520 - no ARP8 orthologue among them, and a different node from ACTR8's. Conversely, ACTR8's nuclear evidence is its own: the IBA rows at PTN000234048 draw on four ARP8 orthologues that each carry their own experimental annotations, the WITH/FROM list includes ACTR8 itself, and the gene independently has IDA, HDA and IEA nuclear rows. The nuclear leak in this family therefore runs through the ARP9/ACTL7 side, not the ARP8 side. Core. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0191 · UniProt subcellular location Nucleus SUPPORTS TRANSFER UniProt subcellular-location vocabulary term Nucleus, mapped to GO:0005634. The underlying UniProt statement is ECO:0000269\|PubMed:18163988, i.e. experimental. Supporting Evidence: file:human/ACTR8/ACTR8-uniprot.txt CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269\|PubMed:18163988}. Chromosome
GO:0005694 chromosome	IEA GO_REF:0000044	ACCEPT	Summary: Correct and deliberately left general. The striking observation is accumulation on mitotic chromosomes, but ARP8 is also on interphase chromatin as an INO80 subunit, so the specific condensed-chromosome term is proposed as an addition rather than a replacement. Reason: SL-0468 maps to GO:0005694 and the underlying UniProt statement is ECO:0000269\|PubMed:18163988, i.e. experimental. A specificity upgrade to GO:0000793 condensed chromosome was considered and rejected as a replacement: hArp8 accumulates on mitotic chromosomes, but it is also required for INO80 recruitment to laser-induced damage in interphase nuclei and works within INO80 during replication and transcription, so restricting the location to the condensed pool would lose the interphase chromatin association. GO:0005694 is therefore the correct cover term and GO:0000793 is proposed separately as a NEW annotation - additive, per the principle that an incomplete but defensible call is better extended than overwritten. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0468 · UniProt subcellular location Chromosome SUPPORTS TRANSFER UniProt subcellular-location vocabulary term Chromosome, mapped to GO:0005694. The underlying UniProt statement is ECO:0000269\|PubMed:18163988, i.e. experimental. Supporting Evidence: PMID:18163988 Here we report that hArp8, but not hArp5, accumulates on mitotic chromosomes. file:human/ACTR8/ACTR8-uniprot.txt Note=Specifically localizes to mitotic
GO:0033044 regulation of chromosome organization	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: True but redundant: an ARBA rule reproducing the ComplexPortal IMP row for the same term, whose evidence is an INO80-complex knockdown rather than an ARP8 experiment. Reason: ARBA:ARBA00029256 gives no traceable per-gene experiment, and the term is already present in this snapshot as a ComplexPortal IMP from PMID:26340092. That paper's manipulation is INO80 RNAi, giving abnormal chromosome stability at the complex level; nothing there tests ARP8. ARP8 does have its own chromosome phenotype - RNAi depletion misaligns mitotic chromosomes - but that is a chromosome-localization process, and GO:0007080 mitotic metaphase chromosome alignment is not a descendant of GO:0033044 (its ancestors include GO:0051276 chromosome organization but not the regulation branch), so it cannot be folded into this row and is proposed separately. Kept as a true, non-core, complex-level statement. GRANULARITY_MISMATCH here means the first sense its definition allows, parent term true but uninformative, not that a child overstates specificity. Propagation Review Root cause: EVIDENCE CIRCULAR OR REDUNDANT Failure modes: SOURCE EVIDENCE WEAK GRANULARITY MISMATCH Sources checked: ARBA:ARBA00029256 · ARBA rule ARBA00029256 SOURCE WEAK OR INFERRED ARBA machine-learning rule; no traceable per-gene experiment. Supporting Evidence: PMID:26340092 RNAi knockdown strategies of INO80 not only led to prolonged progression of cell cycle phase G2/M to G1, but it also resulted in abnormal chromosome stability.
GO:0051052 regulation of DNA metabolic process	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: A true but wholly subsumed parent: both of its relevant children, regulation of DNA replication and regulation of DNA repair, are separately annotated on this gene. Reason: ARP8 does regulate DNA metabolic processes, so the term is not wrong, and MARK_AS_OVER_ANNOTATED would misdescribe it: a redundant true parent is not an over-annotation. It carries no information beyond GO:0006275 and GO:0006282, both present in this snapshot and both is_a descendants of it. Kept as non-core on uninformativeness rather than on correctness; GRANULARITY_MISMATCH is used in the parent-term-is-true-but-uninformative sense. Propagation Review Root cause: EVIDENCE CIRCULAR OR REDUNDANT Failure modes: GRANULARITY MISMATCH SOURCE EVIDENCE WEAK Sources checked: ARBA:ARBA00027282 · ARBA rule ARBA00027282 SOURCE WEAK OR INFERRED ARBA machine-learning rule; no traceable per-gene experiment.
GO:0005515 protein binding	IPI PMID:16230350 A mammalian chromatin remodeling complex with similarities t...	KEEP AS NON CORE	Summary: ARP8-ACTR5, detected in the original purification of the human INO80 complex. Real, but uninformative as a molecular function. Reason: Partner UniProtKB:Q9H9F9 = ACTR5. This is the paper that identified the mammalian INO80 complex, so the contact is a within-complex one recorded from affinity purification and mass spectrometry; IntAct logs 17 records from this publication for ACTR8. Shared basis for all six protein-binding rows, stated once here and evidenced in full in ACTR8-notes.md section 8: both GOA partners are co-members of ACTR8's own complex (ComplexPortal CPX-846 lists 15 participants including Q9H981, Q9H9F9 and Q9Y5K5), so the informative content is already carried by the GO:0031011 part_of rows; both partner accessions resolve to reviewed canonical entries at canonical length (ACTR5 607 aa, UCHL5 329 aa), so no TrEMBL clone or ORFeome fragment is standing in for a named partner; and IntAct returns 82 records across 14 distinct publications, so these are not one screen counted several ways. Kept because the partners are real and replicated, non-core because ARP8's molecular function is the nucleosome, histone and single-stranded DNA binding proposed separately. Consistent with how the merged ACTR1A, ACTR1B and ACTL7A reviews treated real replicated partners; ACTR10 and ACTL7B differ only because their partners were screen singletons - decide per partner is the shared rule. Supporting Evidence: file:human/ACTR8/ACTR8-uniprot.txt CC Q9H981; Q9H9F9: ACTR5; NbExp=3; IntAct=EBI-769597, EBI-769418;
GO:0005515 protein binding	IPI PMID:18163988 The actin-related protein hArp8 accumulates on the mitotic c...	KEEP AS NON CORE	Summary: ARP8-ACTR5 by targeted co-immunoprecipitation, the strongest-scoring of the protein-binding rows and the one that carries a cell-cycle-dependent observation. Reason: Partner UniProtKB:Q9H9F9 = ACTR5. IntAct records this as anti bait coip, physical association, MI-score 0.67 - a targeted experiment, not a proteome map, so the ACRV1 pattern of a single screen logged under several sub-method names does not apply. The interesting content is not the binding but its cell-cycle dependence: UniProt records the interaction in asynchronous interphase cells but not in metaphase-arrested cells, which fits this paper's central finding that hArp8's mitotic chromosome role is INO80-independent. That biology is captured in the proposed GO:0007080 annotation rather than in a protein-binding row. Shared basis for all six protein-binding rows, stated once here and evidenced in full in ACTR8-notes.md section 8: both GOA partners are co-members of ACTR8's own complex (ComplexPortal CPX-846 lists 15 participants including Q9H981, Q9H9F9 and Q9Y5K5), so the informative content is already carried by the GO:0031011 part_of rows; both partner accessions resolve to reviewed canonical entries at canonical length (ACTR5 607 aa, UCHL5 329 aa), so no TrEMBL clone or ORFeome fragment is standing in for a named partner; and IntAct returns 82 records across 14 distinct publications, so these are not one screen counted several ways. Kept because the partners are real and replicated, non-core because ARP8's molecular function is the nucleosome, histone and single-stranded DNA binding proposed separately. Consistent with how the merged ACTR1A, ACTR1B and ACTL7A reviews treated real replicated partners; ACTR10 and ACTL7B differ only because their partners were screen singletons - decide per partner is the shared rule. Supporting Evidence: PMID:18163988 In contrast, depletion of hIno80 and hArp5 did not cause misalignment of chromosomes, suggesting that the role of hArp8 at mitotic chromosomes is independent of the activity of hINO80 complexes.
GO:0005515 protein binding	IPI PMID:18922472 Distinct modes of regulation of the Uch37 deubiquitinating e...	KEEP AS NON CORE	Summary: ARP8-UCHL5 from the dedicated study of Uch37 in the INO80 complex. A real within-complex association. Reason: Partner UniProtKB:Q9Y5K5 = UCHL5 (Uch37), a bona fide CPX-846 participant whose regulation within INO80 is this paper's subject rather than an incidental hit. UniProt records NbExp=5 for the pair and IntAct logs 5 records from this publication. Shared basis for all six protein-binding rows, stated once here and evidenced in full in ACTR8-notes.md section 8: both GOA partners are co-members of ACTR8's own complex (ComplexPortal CPX-846 lists 15 participants including Q9H981, Q9H9F9 and Q9Y5K5), so the informative content is already carried by the GO:0031011 part_of rows; both partner accessions resolve to reviewed canonical entries at canonical length (ACTR5 607 aa, UCHL5 329 aa), so no TrEMBL clone or ORFeome fragment is standing in for a named partner; and IntAct returns 82 records across 14 distinct publications, so these are not one screen counted several ways. Kept because the partners are real and replicated, non-core because ARP8's molecular function is the nucleosome, histone and single-stranded DNA binding proposed separately. Consistent with how the merged ACTR1A, ACTR1B and ACTL7A reviews treated real replicated partners; ACTR10 and ACTL7B differ only because their partners were screen singletons - decide per partner is the shared rule. Supporting Evidence: file:human/ACTR8/ACTR8-uniprot.txt CC Q9H981; Q9Y5K5: UCHL5; NbExp=5; IntAct=EBI-769597, EBI-1051183;
GO:0005515 protein binding	IPI PMID:26496610 A human interactome in three quantitative dimensions organiz...	KEEP AS NON CORE	Summary: ARP8-ACTR5 in a quantitative interactome with stoichiometries. Corroborative. Reason: Partner UniProtKB:Q9H9F9 = ACTR5, here from a large-scale quantitative affinity-purification study rather than a targeted assay. It is corroboration of an already well-established within-complex contact rather than a new claim, so it is neither a screen artefact to flag nor a source of new mechanism. Shared basis for all six protein-binding rows, stated once here and evidenced in full in ACTR8-notes.md section 8: both GOA partners are co-members of ACTR8's own complex (ComplexPortal CPX-846 lists 15 participants including Q9H981, Q9H9F9 and Q9Y5K5), so the informative content is already carried by the GO:0031011 part_of rows; both partner accessions resolve to reviewed canonical entries at canonical length (ACTR5 607 aa, UCHL5 329 aa), so no TrEMBL clone or ORFeome fragment is standing in for a named partner; and IntAct returns 82 records across 14 distinct publications, so these are not one screen counted several ways. Kept because the partners are real and replicated, non-core because ARP8's molecular function is the nucleosome, histone and single-stranded DNA binding proposed separately. Consistent with how the merged ACTR1A, ACTR1B and ACTL7A reviews treated real replicated partners; ACTR10 and ACTL7B differ only because their partners were screen singletons - decide per partner is the shared rule.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: ARP8-UCHL5 in BioPlex-style dual proteome-scale networks. Corroborative. Reason: Partner UniProtKB:Q9Y5K5 = UCHL5. This is the largest single contributor to ACTR8's IntAct record (30 of 82 records), almost all anti tag coip at MI-score 0.35, so most of its partners are low-confidence singletons; the UCHL5 pair is not, because it is independently established by PMID:18922472 and by CPX-846 membership. Judged per partner rather than per publication. Shared basis for all six protein-binding rows, stated once here and evidenced in full in ACTR8-notes.md section 8: both GOA partners are co-members of ACTR8's own complex (ComplexPortal CPX-846 lists 15 participants including Q9H981, Q9H9F9 and Q9Y5K5), so the informative content is already carried by the GO:0031011 part_of rows; both partner accessions resolve to reviewed canonical entries at canonical length (ACTR5 607 aa, UCHL5 329 aa), so no TrEMBL clone or ORFeome fragment is standing in for a named partner; and IntAct returns 82 records across 14 distinct publications, so these are not one screen counted several ways. Kept because the partners are real and replicated, non-core because ARP8's molecular function is the nucleosome, histone and single-stranded DNA binding proposed separately. Consistent with how the merged ACTR1A, ACTR1B and ACTL7A reviews treated real replicated partners; ACTR10 and ACTL7B differ only because their partners were screen singletons - decide per partner is the shared rule.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	KEEP AS NON CORE	Summary: ARP8-UCHL5 in multimodal cell maps. Corroborative. Reason: Partner UniProtKB:Q9Y5K5 = UCHL5, from a proteome-scale map. Same judgement as the other UCHL5 rows: the partner is a real CPX-846 co-member, so the row is not an over-annotation, but it adds no mechanism. The IntAct census produced one result worth recording, and it cuts against these rows rather than for them. Ranking ACTR8's partners by the number of distinct publications supporting them, the top two are YY1 (5 publications, MI-score 0.80) and INO80E (5 publications, MI-score 0.79), with RUVBL1 and RUVBL2 next at 4 publications and 0.73. The two partners GOA actually records sit below all of these: ACTR5 at 3 publications and MI 0.67, UCHL5 at 4 publications with records as low as MI 0.35. So the six GO:0005515 rows under-represent rather than over-represent the interaction data, and the omission of YY1 is the sharpest instance - PMID:18026119 is already cited on this gene for the Ino80-complex IDA and YY1 is the bait that paper used, so the contact is established by a reference GOA already has in hand. Shared basis for all six protein-binding rows, stated once here and evidenced in full in ACTR8-notes.md section 8: both GOA partners are co-members of ACTR8's own complex (ComplexPortal CPX-846 lists 15 participants including Q9H981, Q9H9F9 and Q9Y5K5), so the informative content is already carried by the GO:0031011 part_of rows; both partner accessions resolve to reviewed canonical entries at canonical length (ACTR5 607 aa, UCHL5 329 aa), so no TrEMBL clone or ORFeome fragment is standing in for a named partner; and IntAct returns 82 records across 14 distinct publications, so these are not one screen counted several ways. Kept because the partners are real and replicated, non-core because ARP8's molecular function is the nucleosome, histone and single-stranded DNA binding proposed separately. Consistent with how the merged ACTR1A, ACTR1B and ACTL7A reviews treated real replicated partners; ACTR10 and ACTL7B differ only because their partners were screen singletons - decide per partner is the shared rule.
GO:0000723 telomere maintenance	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: Transferred from mouse Actr8, but the mouse annotation is a ComplexPortal projection of an Ino80-knockout telomere phenotype onto all 15 subunits. No ARP8-specific telomere evidence exists in any organism. Reason: Shared trace for all five GO_REF:0000107 rows, stated once here and evidenced in full in ACTR8-notes.md section 7b. All five of mouse Actr8's annotations from PMID:23979016 are assignedBy ComplexPortal, and QuickGO reference=PMID:23979016 returns 80 annotations = 16 entities x 5 terms: CPX-878 plus all 15 INO80 subunits with byte-identical term and evidence sets. The paper's experiment is an Ino80 conditional knockout, Actr8 is not named in the abstract, and no Actr8 mouse knockout exists. So the mouse IMP/IDA is a complex-level annotation projected onto a subunit, and Ensembl Compara then consumes it as gene-specific mouse experimental evidence and re-projects it onto human ACTR8, losing the complex context: two inferences stacked and presented as one IEA from an orthologue. The orthology itself is sound (Q8R2S9 is reviewed mouse Actr8 at 624 aa, and ensembl:ENSMUSP00000016115 resolves to the same gene rather than an independent source). ComplexPortal's own layer is a documented convention with the complex recoverable from CPX-878; the defect is in the second step. For this term specifically, the underlying result is stated for the complex, not for a subunit, and there is no ARP8-specific telomere experiment in mouse, human or yeast. MARK_AS_OVER_ANNOTATED rather than REMOVE: ARP8 is a core INO80 subunit and I cannot demonstrate that it is dispensable for the complex's telomere function, so the defensible statement is that the gene-level specificity is unearned, not that the biology is false. Recommendation: re-attribute to CPX-846 and drop the Compara-derived gene-level row, or re-issue it with the complex as the annotation subject. Propagation Review Root cause: EVIDENCE CIRCULAR OR REDUNDANT Failure modes: CIRCULAR PROPAGATION ROLE CONFLATION Sources checked: UniProtKB:Q8R2S9 · mouse Actr8 (Q8R2S9) SUPPORTS SOURCE BUT NOT TARGET Q8R2S9 ARP8_MOUSE, mouse Actr8, Swiss-Prot reviewed, 624 aa (identical length to human ACTR8), a genuine 1:1 orthologue. The orthology is sound; what is unsound is the annotation being transferred. All five of mouse Actr8's annotations from PMID:23979016 are assignedBy ComplexPortal, and QuickGO reference=PMID:23979016 returns 80 annotations = 16 entities x 5 terms: CPX-878 plus all 15 INO80 subunits with byte-identical term/evidence sets. The paper's experiment is an Ino80 conditional knockout; Actr8 was not manipulated. ensembl:ENSMUSP00000016115 · mouse Actr8-201 translation SUPPORTS SOURCE BUT NOT TARGET Resolves to transcript ENSMUST00000016115 (Actr8-201), gene ENSMUSG00000015971 = mouse Actr8, i.e. the same entity as UniProtKB:Q8R2S9 rather than an independent source. Same caveat applies. Supporting Evidence: PMID:23979016 Here, we use a conditional knockout approach to explore the cellular and organismal functions of mIno80. PMID:23979016 Our studies suggest that the mIno80 chromatin remodeling complex plays important roles in telomere replication, HDR-mediated repair of dysfunctional telomeres, and maintenance of genome stability.
GO:0006282 regulation of DNA repair	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: The transfer route is unsound, but this term survives on ACTR8's own human evidence: ARP8 is the subunit required for INO80 recruitment to damage sites, and its ATM/ATR-dependent phosphorylation tunes how much INO80 loads there. Reason: Shared trace for all five GO_REF:0000107 rows, stated once here and evidenced in full in ACTR8-notes.md section 7b. All five of mouse Actr8's annotations from PMID:23979016 are assignedBy ComplexPortal, and QuickGO reference=PMID:23979016 returns 80 annotations = 16 entities x 5 terms: CPX-878 plus all 15 INO80 subunits with byte-identical term and evidence sets. The paper's experiment is an Ino80 conditional knockout, Actr8 is not named in the abstract, and no Actr8 mouse knockout exists. So the mouse IMP/IDA is a complex-level annotation projected onto a subunit, and Ensembl Compara then consumes it as gene-specific mouse experimental evidence and re-projects it onto human ACTR8, losing the complex context: two inferences stacked and presented as one IEA from an orthologue. The orthology itself is sound (Q8R2S9 is reviewed mouse Actr8 at 624 aa, and ensembl:ENSMUSP00000016115 resolves to the same gene rather than an independent source). ComplexPortal's own layer is a documented convention with the complex recoverable from CPX-878; the defect is in the second step. Unlike the telomere and embryonic-development rows, this one does not depend on the bad route. Among the INO80 subunits tested by RNAi, only ARP8 was indispensable for recruiting the complex to laser-induced damage sites, and ARP8 phosphorylation by ATM and ATR modulates INO80 and RAD51 loading at break sites - so ARP8 sits inside a regulatory step of repair, in both directions. Kept, and marked non-core because the core statement is the direct one, GO:0006302 double-strand break repair, which ACTR8 already carries; the regulation-level parent is the derived reading. The actionable item is to re-base the evidence on the human papers rather than on the Compara transfer. Propagation Review Root cause: EVIDENCE CIRCULAR OR REDUNDANT Failure modes: CIRCULAR PROPAGATION ROLE CONFLATION Sources checked: UniProtKB:Q8R2S9 · mouse Actr8 (Q8R2S9) SUPPORTS SOURCE BUT NOT TARGET Q8R2S9 ARP8_MOUSE, mouse Actr8, Swiss-Prot reviewed, 624 aa (identical length to human ACTR8), a genuine 1:1 orthologue. The orthology is sound; what is unsound is the annotation being transferred. All five of mouse Actr8's annotations from PMID:23979016 are assignedBy ComplexPortal, and QuickGO reference=PMID:23979016 returns 80 annotations = 16 entities x 5 terms: CPX-878 plus all 15 INO80 subunits with byte-identical term/evidence sets. The paper's experiment is an Ino80 conditional knockout; Actr8 was not manipulated. ensembl:ENSMUSP00000016115 · mouse Actr8-201 translation SUPPORTS SOURCE BUT NOT TARGET Resolves to transcript ENSMUST00000016115 (Actr8-201), gene ENSMUSG00000015971 = mouse Actr8, i.e. the same entity as UniProtKB:Q8R2S9 rather than an independent source. Same caveat applies. Supporting Evidence: PMID:20971067 we show that the mammalian INO80 complex is recruited to the laser-induced DNA damage sites in a phosphorylated H2AX PMID:29759113 The etoposide-induced phosphorylation of ARP8 is regulated by ATM and ATR, and attenuates its interaction with INO80.
GO:0045739 positive regulation of DNA repair	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Same unsound route as the other Compara rows, but the positive sign is independently supported: loss of ARP8 impairs repair, so ARP8's net contribution is positive. Reason: Shared trace for all five GO_REF:0000107 rows, stated once here and evidenced in full in ACTR8-notes.md section 7b. All five of mouse Actr8's annotations from PMID:23979016 are assignedBy ComplexPortal, and QuickGO reference=PMID:23979016 returns 80 annotations = 16 entities x 5 terms: CPX-878 plus all 15 INO80 subunits with byte-identical term and evidence sets. The paper's experiment is an Ino80 conditional knockout, Actr8 is not named in the abstract, and no Actr8 mouse knockout exists. So the mouse IMP/IDA is a complex-level annotation projected onto a subunit, and Ensembl Compara then consumes it as gene-specific mouse experimental evidence and re-projects it onto human ACTR8, losing the complex context: two inferences stacked and presented as one IEA from an orthologue. The orthology itself is sound (Q8R2S9 is reviewed mouse Actr8 at 624 aa, and ensembl:ENSMUSP00000016115 resolves to the same gene rather than an independent source). ComplexPortal's own layer is a documented convention with the complex recoverable from CPX-878; the defect is in the second step. The positive direction stands on human data independent of the transfer: a conditional human ARP8 knockout is hypersensitive to aphidicolin and camptothecin, i.e. removing ARP8 makes repair worse. One caveat is recorded rather than suppressed: ARP8 also has a negative arm, since its ATM-regulated phosphorylation reduces excessive INO80 and RAD51 loading at the breakpoint cluster region, so ARP8 is not purely a positive regulator. That is why the direction-neutral GO:0006282 is the safer of the two rows and this signed child is kept as non-core rather than accepted as core. Propagation Review Root cause: EVIDENCE CIRCULAR OR REDUNDANT Failure modes: CIRCULAR PROPAGATION ROLE CONFLATION Sources checked: UniProtKB:Q8R2S9 · mouse Actr8 (Q8R2S9) SUPPORTS SOURCE BUT NOT TARGET Q8R2S9 ARP8_MOUSE, mouse Actr8, Swiss-Prot reviewed, 624 aa (identical length to human ACTR8), a genuine 1:1 orthologue. The orthology is sound; what is unsound is the annotation being transferred. All five of mouse Actr8's annotations from PMID:23979016 are assignedBy ComplexPortal, and QuickGO reference=PMID:23979016 returns 80 annotations = 16 entities x 5 terms: CPX-878 plus all 15 INO80 subunits with byte-identical term/evidence sets. The paper's experiment is an Ino80 conditional knockout; Actr8 was not manipulated. ensembl:ENSMUSP00000016115 · mouse Actr8-201 translation SUPPORTS SOURCE BUT NOT TARGET Resolves to transcript ENSMUST00000016115 (Actr8-201), gene ENSMUSG00000015971 = mouse Actr8, i.e. the same entity as UniProtKB:Q8R2S9 rather than an independent source. Same caveat applies. Supporting Evidence: PMID:25299602 This result suggests that knockout of Arp8 probably impairs DNA repair, which probably takes place via the HR or an HR-like repair process. PMID:29759113 The ATM-regulated phosphorylation of ARP8 reduces the excessive loading of INO80 and RAD51 onto the breakpoint cluster region.
GO:0045995 regulation of embryonic development	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: The datum behind this row is that Ino80-null mouse embryos die early. That is an Ino80 gene phenotype projected to 15 subunits and then across species; ARP8 has no embryonic phenotype of its own. Reason: Shared trace for all five GO_REF:0000107 rows, stated once here and evidenced in full in ACTR8-notes.md section 7b. All five of mouse Actr8's annotations from PMID:23979016 are assignedBy ComplexPortal, and QuickGO reference=PMID:23979016 returns 80 annotations = 16 entities x 5 terms: CPX-878 plus all 15 INO80 subunits with byte-identical term and evidence sets. The paper's experiment is an Ino80 conditional knockout, Actr8 is not named in the abstract, and no Actr8 mouse knockout exists. So the mouse IMP/IDA is a complex-level annotation projected onto a subunit, and Ensembl Compara then consumes it as gene-specific mouse experimental evidence and re-projects it onto human ACTR8, losing the complex context: two inferences stacked and presented as one IEA from an orthologue. The orthology itself is sound (Q8R2S9 is reviewed mouse Actr8 at 624 aa, and ensembl:ENSMUSP00000016115 resolves to the same gene rather than an independent source). ComplexPortal's own layer is a documented convention with the complex recoverable from CPX-878; the defect is in the second step. This is the clearest case in the group, because the phenotype is explicitly attributed to the Ino80 gene: mIno80-null embryos die early during embryogenesis. No Actr8 mouse knockout exists, and the only ARP8-null system available is a tetracycline-inducible human cell line, which is viable with reduced growth rather than dead - the opposite end of the severity scale from embryonic lethality, though in a cell line rather than an animal, so it is not a refutation. MARK_AS_OVER_ANNOTATED, not REMOVE: the term is not demonstrably false for a core subunit of an essential complex, it is simply not established for this gene. Propagation Review Root cause: EVIDENCE CIRCULAR OR REDUNDANT Failure modes: CIRCULAR PROPAGATION ROLE CONFLATION Sources checked: UniProtKB:Q8R2S9 · mouse Actr8 (Q8R2S9) SUPPORTS SOURCE BUT NOT TARGET Q8R2S9 ARP8_MOUSE, mouse Actr8, Swiss-Prot reviewed, 624 aa (identical length to human ACTR8), a genuine 1:1 orthologue. The orthology is sound; what is unsound is the annotation being transferred. All five of mouse Actr8's annotations from PMID:23979016 are assignedBy ComplexPortal, and QuickGO reference=PMID:23979016 returns 80 annotations = 16 entities x 5 terms: CPX-878 plus all 15 INO80 subunits with byte-identical term/evidence sets. The paper's experiment is an Ino80 conditional knockout; Actr8 was not manipulated. ensembl:ENSMUSP00000016115 · mouse Actr8-201 translation SUPPORTS SOURCE BUT NOT TARGET Resolves to transcript ENSMUST00000016115 (Actr8-201), gene ENSMUSG00000015971 = mouse Actr8, i.e. the same entity as UniProtKB:Q8R2S9 rather than an independent source. Same caveat applies. Supporting Evidence: PMID:23979016 mouse embryos die early during embryogenesis, while conditional deletion of mIno80 in adult mice results in weight loss and premature death PMID:25299602 This result suggests that Arp8 is required for normal cell growth.
GO:1904507 positive regulation of telomere maintenance in response to DNA damage	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: The most specific of the five Compara rows and the least earned: a highly precise claim about ARP8 built from an Ino80-knockout telomere result, via a complex-to-subunit projection. Reason: Shared trace for all five GO_REF:0000107 rows, stated once here and evidenced in full in ACTR8-notes.md section 7b. All five of mouse Actr8's annotations from PMID:23979016 are assignedBy ComplexPortal, and QuickGO reference=PMID:23979016 returns 80 annotations = 16 entities x 5 terms: CPX-878 plus all 15 INO80 subunits with byte-identical term and evidence sets. The paper's experiment is an Ino80 conditional knockout, Actr8 is not named in the abstract, and no Actr8 mouse knockout exists. So the mouse IMP/IDA is a complex-level annotation projected onto a subunit, and Ensembl Compara then consumes it as gene-specific mouse experimental evidence and re-projects it onto human ACTR8, losing the complex context: two inferences stacked and presented as one IEA from an orthologue. The orthology itself is sound (Q8R2S9 is reviewed mouse Actr8 at 624 aa, and ensembl:ENSMUSP00000016115 resolves to the same gene rather than an independent source). ComplexPortal's own layer is a documented convention with the complex recoverable from CPX-878; the defect is in the second step. The specificity is the problem. GO:1904507 asserts that ACTR8 positively regulates telomere maintenance specifically in response to DNA damage - three conjoined claims, none of which has been tested on ARP8 in any organism. The parent GO:0000723 on the same route is already flagged; a child that adds a damage-response restriction on top of an untested parent compounds rather than refines. GRANULARITY_MISMATCH here means the second sense its definition allows, the child term overstates specificity, not that a parent is uninformative. Not REMOVE, for the same reason as the other two: ARP8 is a core INO80 subunit and no experiment excludes it from this function. Propagation Review Root cause: EVIDENCE CIRCULAR OR REDUNDANT Failure modes: CIRCULAR PROPAGATION ROLE CONFLATION GRANULARITY MISMATCH Sources checked: UniProtKB:Q8R2S9 · mouse Actr8 (Q8R2S9) SUPPORTS SOURCE BUT NOT TARGET Q8R2S9 ARP8_MOUSE, mouse Actr8, Swiss-Prot reviewed, 624 aa (identical length to human ACTR8), a genuine 1:1 orthologue. The orthology is sound; what is unsound is the annotation being transferred. All five of mouse Actr8's annotations from PMID:23979016 are assignedBy ComplexPortal, and QuickGO reference=PMID:23979016 returns 80 annotations = 16 entities x 5 terms: CPX-878 plus all 15 INO80 subunits with byte-identical term/evidence sets. The paper's experiment is an Ino80 conditional knockout; Actr8 was not manipulated. ensembl:ENSMUSP00000016115 · mouse Actr8-201 translation SUPPORTS SOURCE BUT NOT TARGET Resolves to transcript ENSMUST00000016115 (Actr8-201), gene ENSMUSG00000015971 = mouse Actr8, i.e. the same entity as UniProtKB:Q8R2S9 rather than an independent source. Same caveat applies. Supporting Evidence: PMID:23979016 Our studies suggest that the mIno80 chromatin remodeling complex plays important roles in telomere replication, HDR-mediated repair of dysfunctional telomeres, and maintenance of genome stability. PMID:23979016 While mIno80 is required for efficient repair of DNA double strand breaks
GO:0006275 regulation of DNA replication	IMP PMID:25016522 The mammalian INO80 chromatin remodeling complex is required...	ACCEPT	Summary: One of the few ComplexPortal rows where the cited paper actually assayed ARP8: cells deficient for Arp8, not only for Ino80, failed to restart replication after stress. Reason: This row was checked for the usual complex-level substitution and it passes. The paper's fibre- and bulk-labelling experiments were done on cells deficient for Ino80 and Arp8, so the gene-level IMP is genuinely gene-level. It is corroborated independently by the human ARP8 conditional knockout, which is hypersensitive to aphidicolin, a replication inhibitor. Accepted as core: replication-stress recovery is one of the established functions of the ARP8-containing INO80 complex, and ARP8 is on the measured side of it rather than merely present in the complex. Supporting Evidence: PMID:25016522 we found that cells deficient for Ino80 and Arp8 had impaired replication restart after treatment with replication inhibitors and accumulated double-strand breaks PMID:25299602 This result suggests that knockout of Arp8 probably impairs DNA repair, which probably takes place via the HR or an HR-like repair process.
GO:0006338 chromatin remodeling	IDA PMID:21303910 Subunit organization of the human INO80 chromatin remodeling...	ACCEPT	Summary: ARP8 is in the module that is required for ATP-dependent nucleosome remodelling by the human complex, and a recombinant human core containing ARP8 slides nucleosomes. Reason: The paper resolves the human complex into three modules and places Arp4 and Arp8 with the Ino80 HSA/PTH and Snf2 ATPase domains and YY1 in the module that is required for remodelling, in explicit contrast to the metazoan-specific module which is not. Remodelling activity is attributed to the core comprising those domains together with the complete set of evolutionarily conserved subunits, and ARP8 is one of those subunits. Independently, a reconstituted human minimal core containing Arp8 has nucleosome-sliding activity comparable to the endogenous complex. Core as a biological process. Note deliberately what is not claimed: the remodeller molecular function belongs to the INO80 ATPase, not to ARP8, so no ATP-dependent chromatin-remodeller MF is proposed for this gene - ARP8's own measured activities are the binding activities proposed as new terms. Supporting Evidence: PMID:21303910 ATP-dependent nucleosome remodeling by the hINO80 complex is catalyzed by a core complex comprising the hIno80 protein HSA/PTH and Snf2 ATPase domains acting in concert with YY1 and the complete set of its evolutionarily conserved subunits PMID:27257055 This core complex has nucleosome sliding activity that is similar to that of endogenous human and yeast Ino80 complexes
GO:0031011 Ino80 complex	IDA PMID:21303910 Subunit organization of the human INO80 chromatin remodeling...	ACCEPT	Summary: Direct assay of subunit composition in the human complex. Correct and core. Note this identical row appears twice in the GOA TSV, once from ComplexPortal and once from UniProt. Reason: The paper dissects human INO80 into modules by purifying subassemblies, so ARP8's membership is directly assayed rather than inferred. ComplexPortal CPX-846 lists ACTR8 among 15 participants. A minor data-hygiene observation for GOA rather than a curation defect: this exact term/evidence/reference triple occurs twice in the downloaded TSV, differing only in the ASSIGNED BY column (ComplexPortal and UniProt), so the same fact is banked twice. Supporting Evidence: PMID:21303910 the actin-related proteins Arp4 and Arp8, and the GLI-Kruppel family transcription factor YY1
GO:0033044 regulation of chromosome organization	IMP PMID:26340092 Negative Regulation of p21Waf1/Cip1 by Human INO80 Chromatin...	KEEP AS NON CORE	Summary: True at the complex level from INO80 RNAi, but ARP8 itself was not manipulated in this paper. ARP8's own chromosome phenotype is more specific and sits outside this term's subtree. Reason: The evidence route is complex-level rather than ARP8-specific: ComplexPortal annotates the INO80 complex and projects the term to every subunit, so the datum behind this row is a manipulation of the complex, not of ARP8. Here the manipulation is INO80 RNAi in HeLa cells, giving abnormal chromosome stability alongside a G2/M delay; ARP8 is not among the genes knocked down. The row is not overruled - a curator reading the full text made a defensible complex-level call, and CLAUDE.md is explicit that an experimental annotation should not be second-guessed from an abstract - but it is marked non-core because ARP8's own, INO80-independent chromosome phenotype is a different and more specific thing: RNAi depletion of hArp8 misaligns mitotic chromosomes, while depletion of hIno80 and hArp5 does not. That belongs at GO:0007080, which is not a descendant of GO:0033044, and is proposed as a new annotation. Supporting Evidence: PMID:26340092 RNAi knockdown strategies of INO80 not only led to prolonged progression of cell cycle phase G2/M to G1, but it also resulted in abnormal chromosome stability. PMID:18163988 In contrast, depletion of hIno80 and hArp5 did not cause misalignment of chromosomes, suggesting that the role of hArp8 at mitotic chromosomes is independent of the activity of hINO80 complexes.
GO:0045893 positive regulation of DNA-templated transcription	IMP PMID:27641337 INO80 is required for oncogenic transcription and tumor grow...	KEEP AS NON CORE	Summary: The signed child of a function the complex performs in both directions, from an INO80-silencing experiment in lung cancer cells. Kept, but non-core. Reason: The evidence route is complex-level rather than ARP8-specific: ComplexPortal annotates the INO80 complex and projects the term to every subunit, so the datum behind this row is a manipulation of the complex, not of ARP8. In this paper the manipulation is INO80 silencing, and the subunits discussed are Ino80 and Ino80B; ARP8 is not named in the abstract. The row is not overruled, because the cached record is abstract-only and the curator read the full text. It is non-core for two reasons that are independent of the evidence route. First, the complex regulates transcription in both directions - it activates at enhancers here and represses p21 elsewhere - so a signed term captures one context rather than the function; the direction-neutral parent GO:0006355, which ACTR8 also carries and which is accepted as core, is the correct general statement. Second, transcriptional output is downstream of the remodelling activity that ARP8 actually contributes to. Supporting Evidence: PMID:27641337 Here we show that the INO80 chromatin remodeling complex is required for oncogenic transcription and tumor growth in non-small-cell lung cancer (NSCLC). PMID:26340092 we first demonstrate that INO80 complex negatively regulates the p21Waf1/Cip1 (p21) expression in a p53-mediated mechanism
GO:0051726 regulation of cell cycle	IMP PMID:26340092 Negative Regulation of p21Waf1/Cip1 by Human INO80 Chromatin...	KEEP AS NON CORE	Summary: A downstream, complex-level consequence: INO80 RNAi delays G2/M-to-G1 progression. True but several steps from ARP8's molecular activity. Reason: The evidence route is complex-level rather than ARP8-specific: ComplexPortal annotates the INO80 complex and projects the term to every subunit, so the datum behind this row is a manipulation of the complex, not of ARP8. The cell-cycle delay follows from p21 de-repression after INO80 knockdown, so it is two steps downstream: complex loss, then transcriptional change, then cell-cycle effect. ARP8 does have cell-cycle-adjacent phenotypes of its own - a conditional knockout grows poorly, and RNAi depletion misaligns mitotic chromosomes - but those are better served by the specific terms proposed elsewhere in this review than by a generic regulation-of-cell-cycle row. Kept as a true pleiotropic statement, not core. Supporting Evidence: PMID:26340092 RNAi knockdown strategies of INO80 not only led to prolonged progression of cell cycle phase G2/M to G1, but it also resulted in abnormal chromosome stability.
GO:0060382 regulation of DNA strand elongation	IMP PMID:25016522 The mammalian INO80 chromatin remodeling complex is required...	ACCEPT	Summary: The specific reading of the same ARP8-inclusive fibre-labelling experiment behind the regulation-of-DNA-replication row, and the term definition matches what was measured. Reason: GO:0060382's definition is modulation of DNA strand elongation, the process in which an existing strand is extended by nucleotide addition at the 3' end - which is what DNA fibre labelling measures. The experiment used cells deficient for Ino80 and Arp8, so ARP8 is on the measured side, and the paper separates elongation from initiation explicitly, reporting a requirement for the former and not the latter. Accepted as core alongside GO:0006275, both from the same ARP8-inclusive experiment: the parent states the replication role and this child states which step. The definition was read rather than the label, because 'strand elongation' could equally have meant a transcription or repair-synthesis step. Supporting Evidence: PMID:25016522 We report that INO80 was specifically needed for efficient replication elongation, while it was not required for initiation of replication. PMID:25016522 we found that cells deficient for Ino80 and Arp8 had impaired replication restart after treatment with replication inhibitors and accumulated double-strand breaks
GO:0005654 nucleoplasm	IDA GO_REF:0000052	ACCEPT	Summary: HPA immunofluorescence localising ARP8 to the nucleoplasm. Consistent and core. Reason: An independent imaging-based localisation that agrees with the UniProt nucleus statement, the PMID:18026119 IDA and the sperm-nucleus HDA, and is the compartment in which the INO80 complex acts on chromatin. HPA lists ACTR8 as having low tissue specificity, consistent with a housekeeping chromatin-remodeller subunit rather than a restricted one.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-5689544	ACCEPT	Summary: Reactome's compartment assignment for the reaction UCHL5 binds INO80 complex. Correct but redundant with the HPA IDA. Reason: A traceable author statement derived from placing the reaction 'UCHL5 binds INO80 complex' in the nucleoplasm rather than from a direct observation of ARP8. The compartment is nonetheless right and is independently established by the HPA IDA on the same term, so this is accepted for consistency with that row rather than split off as non-core on the strength of its evidence code. It corroborates one thing usefully: Reactome, ComplexPortal CPX-846 and the GOA protein-binding rows all agree that UCHL5 belongs with the INO80 complex, which is part of why those partner rows were judged real within-complex contacts rather than screen noise.
GO:0005634 nucleus	HDA PMID:21630459 Proteomic characterization of the human sperm nucleus.	ACCEPT	Summary: ARP8 detected by mass spectrometry in purified human sperm nuclei, independently corroborating the nuclear localisation in a second cell type. Reason: The study isolated sperm nuclei to over 99.9% purity and identified 403 proteins, so the compartment call is well controlled for a proteomics experiment, and it agrees with the imaging-based rows on the same term. Accepted rather than kept as non-core for consistency with the other two GO:0005634 rows: nuclear localisation is core for ARP8 regardless of which evidence code establishes it, and coreness is a property of the term for this gene rather than of the assay. What is deliberately not drawn from this row is any functional inference about spermatogenesis - a proteomic detection in sperm nuclei says where the protein is, not what it does there, and that is the trap the testis-enriched members of this same actin family invite. Supporting Evidence: PMID:21630459 403 different proteins have been identified from the isolated sperm nuclei
GO:0005634 nucleus	IDA PMID:18026119 A YY1-INO80 complex regulates genomic stability through homo...	ACCEPT	Summary: Direct nuclear localisation from the YY1-INO80 study. Correct and core. Reason: This is the paper that identified a YY1-containing complex with INO80 components and tied both to homologous-recombination repair, so ARP8's nuclear localisation is observed in the context in which the complex functions. Concordant with the UniProt experimental statement, the HPA nucleoplasm IDA and the sperm-nucleus HDA. Core.
GO:0031011 Ino80 complex	IDA PMID:18026119 A YY1-INO80 complex regulates genomic stability through homo...	ACCEPT	Summary: Second independent IDA for INO80-complex membership, from the YY1-INO80 purification. Correct and core. Reason: Independent of PMID:21303910: a different group, a different purification strategy (YY1 as the entry point) and a different biological question, both placing ARP8 in the complex. Together with the Drosophila, S. pombe and S. cerevisiae experimental annotations traced for the IBA row, INO80-complex membership is the single best-evidenced fact about this gene. Core. Supporting Evidence: PMID:18026119 Further biochemical analyses identified a YY1 complex comprising components of the evolutionarily conserved INO80 chromatin-remodeling complex.
GO:0031491 nucleosome binding	IDA PMID:22977180 Structure of Actin-related protein 8 and its contribution to...	NEW	Summary: ARP8's defining molecular activity, measured on the purified human protein: Kd,app 51.0 +/- 9.6 nM for a 207-bp nucleosome. The paper's own conclusion is that ARP8 functions as a nucleosome recognition module, and GOA records no nucleosome-binding function for this gene. The authors do report cooperativity, but it is not what this term rests on - see the reason. Reason: This is the activity the gene is characterised for and it is entirely absent from GOA. Quantitative fluorescence titrations on full-length human ARP8 and on the delta-1-33 crystallisation construct give closely similar affinities for a 207-bp nucleosome, 51.0 +/- 9.6 nM and 62.6 +/- 16 nM. The qualifier is enables rather than contributes_to because the measurement was made on human ARP8 alone, so it independently possesses the activity - the schema reserves contributes_to for subunits that do not. Two things this row deliberately does NOT claim, because PMID:22977180's Table 2 mixes species and the paper separates them explicitly, assaying full-length and N-terminally truncated human Arp8 as well as yeast Arp8, Arp4 and the Arp8-Arp4-actin-HSA sub-complex. First, no fractional attribution of the module's affinity to ARP8. The Arp8-Arp4-actin-HSA sub-complex measured at 63.6 +/- 6.2 nM is the S. cerevisiae one, so setting it beside the 51 nM human figure would be a cross-species comparison; matched within yeast the comparison inverts, because ScArp8 alone binds the same 207-bp nucleosome at 314 +/- 35 nM, i.e. the module binds roughly 5-fold tighter than ScArp8 alone. ARP8's fractional contribution therefore cannot be derived from these data, and the defensible statement is the authors' own hedged one, that the contribution is significant. Second, cooperativity is not leaned on: human full-length ARP8 gives a Hill coefficient of 1.31 +/- 0.4 for the nucleosome, which overlaps 1, and the unambiguous values are the delta-1-33 construct at 2.11 +/- 0.4 and the yeast sub-complex at 3.13 +/- 0.7. The paper does state cooperative binding of more than one Arp8 per nucleosome and that is quoted, but this term rests on the affinity, not on the Hill coefficient. Discriminating control, with its species named: S. cerevisiae Arp4 shows the opposite preference in the same titration series, binding free (H3-H4)2 at 74.3 +/- 10 nM against 204 +/- 67 nM for the nucleosome. The contrast is real and shows the assay distinguishes nucleosome recognition from histone recognition rather than reporting generic stickiness, but it is a cross-species contrast and is labelled as one. Context for all six proposed rows: a QuickGO query for Q9H981 with aspect=molecular_function returns 7 annotations - six GO:0005515 protein binding IPIs and one GO:0003729 mRNA binding IBA - and an explicit query for GO:0005524 with goUsage=descendants returns zero. So the entire molecular-function description of a protein with a 2.6 A ATP-bound crystal structure, a measured ATPase and published nanomolar dissociation constants is 'protein binding' six times plus one yeast-derived RNA inference. The GO:0005524 IEA:UniProtKB-KW line still present in UniProt's DR block is absent from GOA, consistent with the withdrawal of the Swiss-Prot-keyword route (GO_REF:0000043) that also removed cell division, DNA recombination and DNA-templated transcription from this gene. The merged ACTR1A review independently documents the same pipeline retirement for its paralog, so this is a systematic gap rather than a per-gene oversight. Supporting Evidence: PMID:22977180 strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting that Arp8 functions as a nucleosome recognition module PMID:22977180 Arp8, Arp4 and the INO80 sub-complex I bind (H3–H4)2 and nucleosomes with high affinity PMID:22977180 We conclude that the contribution of Arp8 to the nucleosome-binding ability of INO80 is significant. file:human/ACTR8/ACTR8-uniprot.txt it may act as a nucleosome recognition module within the complex.
GO:0042393 histone binding	IDA PMID:22977180 Structure of Actin-related protein 8 and its contribution to...	NEW	Summary: Human ARP8 binds the (H3-H4)2 histone tetramer at about 110 nM, roughly 5-fold better than the H2A-H2B dimer at about 555 nM. The preference, not just the binding, is the curatable fact. Reason: Measured directly on purified human ARP8 in the same titration series as the nucleosome affinities, so enables is the correct qualifier. The specific preference for the H3-H4 tetramer over the H2A-H2B dimer is what makes ARP8 a recognition module for the intact nucleosome rather than for disassembly intermediates, and it is preserved from yeast to human. GO has no descendant of GO:0042393 that expresses 'H3-H4 tetramer binding' as distinct from binding H3 or H4 individually, and the measurement is on the tetramer as a unit, so the general term is the honest choice rather than a specificity failure - no child of GO:0042393 matches what was assayed. Context for all six proposed rows: a QuickGO query for Q9H981 with aspect=molecular_function returns 7 annotations - six GO:0005515 protein binding IPIs and one GO:0003729 mRNA binding IBA - and an explicit query for GO:0005524 with goUsage=descendants returns zero. So the entire molecular-function description of a protein with a 2.6 A ATP-bound crystal structure, a measured ATPase and published nanomolar dissociation constants is 'protein binding' six times plus one yeast-derived RNA inference. The GO:0005524 IEA:UniProtKB-KW line still present in UniProt's DR block is absent from GOA, consistent with the withdrawal of the Swiss-Prot-keyword route (GO_REF:0000043) that also removed cell division, DNA recombination and DNA-templated transcription from this gene. The merged ACTR1A review independently documents the same pipeline retirement for its paralog, so this is a systematic gap rather than a per-gene oversight. Supporting Evidence: PMID:22977180 All Arp8 variants bind (H3–H4)2 and nucleosomes with comparable affinity, while the interaction with H2A–H2B is PMID:22977180 Arp8 binds (H3–H4)2 with high affinity, and this property is to a large part responsible for its interaction with nucleosomes
GO:0003697 single-stranded DNA binding	IDA PMID:25299602 DNA binding properties of the actin-related protein Arp8 and...	NEW	Summary: Recombinant human ARP8 binds DNA and prefers single-stranded DNA over duplex in a direct three-way competition, with 3'-overhang substrate intermediate. GOA gives ACTR8 no DNA-binding function of any kind. Reason: The specific term is proposed rather than the general GO:0003677 DNA binding because the specificity was measured, not assumed: a competitive gel shift with dsDNA, 3'-overhang DNA and ssDNA present at equal molar ratios shows ssDNA bound first, the overhang intermediate, duplex last. That ordering is also the mechanistically meaningful one - resection at a double-strand break generates exactly this substrate series - and it is the authors' proposed explanation for ARP8 being the subunit required to recruit INO80 to breaks. The activity maps to the basic N-terminal extension: deleting residues 1-38 abolishes the duplex shift and weakens the ssDNA shift. One qualification is recorded rather than suppressed, because it bounds the claim: against a short 30-bp duplex the affinity of human ARP8 is only micromolar (6938 +/- 3448 nM), and the substantial DNA binding of the reconstituted sub-complex - 366 +/- 23 nM, and that is the S. cerevisiae Arp8-Arp4-actin-HSA module, not a human one - was attributed mainly to the INO80 HSA/DBINO domain with only a possible minor Arp8 contribution. The two results are most likely reconciled by substrate length, since 30 bp is too short to engage the extension, but that has not been tested directly - it is filed as a knowledge gap. The term is proposed on the ssDNA gel-shift data, which is unambiguous and is the physiologically relevant ligand. Context for all six proposed rows: a QuickGO query for Q9H981 with aspect=molecular_function returns 7 annotations - six GO:0005515 protein binding IPIs and one GO:0003729 mRNA binding IBA - and an explicit query for GO:0005524 with goUsage=descendants returns zero. So the entire molecular-function description of a protein with a 2.6 A ATP-bound crystal structure, a measured ATPase and published nanomolar dissociation constants is 'protein binding' six times plus one yeast-derived RNA inference. The GO:0005524 IEA:UniProtKB-KW line still present in UniProt's DR block is absent from GOA, consistent with the withdrawal of the Swiss-Prot-keyword route (GO_REF:0000043) that also removed cell division, DNA recombination and DNA-templated transcription from this gene. The merged ACTR1A review independently documents the same pipeline retirement for its paralog, so this is a systematic gap rather than a per-gene oversight. Supporting Evidence: PMID:25299602 we showed that recombinant human Arp8 binds to DNAs, and preferentially binds to single-stranded DNA PMID:25299602 Gel shift assay revealed that indeed Arp8 forms a stable complex with the ssDNA PMID:25299602 These results suggest that Arp8 binds preferentially to ssDNA and that this property likely contributes to recruiting the INO80 complex to the DSB sites PMID:25299602 which lacked the N-terminal extension, was unable to cause any shift in the DNA mobility
GO:0005524 ATP binding	IDA PMID:22977180 Structure of Actin-related protein 8 and its contribution to...	NEW	Summary: ATP is resolved in the human ARP8 crystal structure, and nucleotide occupancy has a demonstrated functional consequence: ATP inhibits ARP8's DNA binding, and the inhibition is lost in pocket mutants. ACTR8 currently has no nucleotide-binding annotation at all. Reason: Annotating the ligand actually observed. PDB 4FO0 is human ARP8 itself - not a homology model and not a paralog - and the structure was solved in the ATP-bound form, with a simulated-annealing omit map computed for the bound ATP. UniProt's BINDING features at 55, 56 and 283-286 carry no ECO:0000250 tag, i.e. they come from this structure rather than by transfer, so the residue evidence is not itself an inference that needs re-testing. The pocket is functional rather than vestigial on two independent counts: human ARP8 hydrolyses ATP at a low basal rate in a 32P assay while yeast Arp4 does not hydrolyse above background - the species qualifier is the source's own, Figure 3's caption reading yeast and human Arp8 but not yeast Arp4 - and ATP, but not ADP, inhibits ARP8 DNA binding, with the inhibition abolished in the S55A/T56A and K288A/S290A mutants, i.e. in exactly the residues UniProt annotates. Residue check in the other direction, so the positive is not over-read: the filament interface is not conserved and the activation residues are substituted (actin Gln137 to Glu266, actin His73 to Arg187), which is why no polymerisation or cytoskeletal term is proposed and why GO:0016887 ATP hydrolysis activity is deliberately withheld despite having been measured. Method consistency with the merged siblings: ACTR1A and ACTR1B proposed GO:0043531 ADP binding because ADP is what their structures resolve, and the now-merged ACTR10 review proposed GO:0005524 with evidence_type ISS because its nucleotide site had to be reconstructed by transferring beta-actin's ATP contacts across an alignment. ARP8 needs no alignment: its own structure resolves ATP, which is why this row is IDA and not ISS. Same rule, different observation, stronger evidence - not a divergence. Context for all six proposed rows: a QuickGO query for Q9H981 with aspect=molecular_function returns 7 annotations - six GO:0005515 protein binding IPIs and one GO:0003729 mRNA binding IBA - and an explicit query for GO:0005524 with goUsage=descendants returns zero. So the entire molecular-function description of a protein with a 2.6 A ATP-bound crystal structure, a measured ATPase and published nanomolar dissociation constants is 'protein binding' six times plus one yeast-derived RNA inference. The GO:0005524 IEA:UniProtKB-KW line still present in UniProt's DR block is absent from GOA, consistent with the withdrawal of the Swiss-Prot-keyword route (GO_REF:0000043) that also removed cell division, DNA recombination and DNA-templated transcription from this gene. The merged ACTR1A review independently documents the same pipeline retirement for its paralog, so this is a systematic gap rather than a per-gene oversight. Supporting Evidence: PMID:22977180 We report the crystal structure of the INO80 complex subunit Arp8 in its ATP-bound form. PMID:22977180 In summary, the intact nucleotide-binding site suggests that Arp8, like actin, is an extremely weak ATPase in a monomeric state. PMID:25299602 addition of ATP significantly inhibited the DNA binding activity of the wild-type Arp8 PMID:25299602 these results suggest that the S55, T56, K288, and S290 residues of Arp8, all of which are located in the ATP binding pocket, might play some regulatory role in the binding of Arp8 to DNA in the presence of ATP file:human/ACTR8/ACTR8-uniprot.txt FT BINDING 55 file:human/ACTR8/ACTR8-uniprot.txt DR PDB; 4FO0; X-ray; 2.60 A; A=34-624.
GO:0007080 mitotic metaphase chromosome alignment	IMP PMID:18163988 The actin-related protein hArp8 accumulates on the mitotic c...	NEW	Summary: The one ARP8 function with no representation anywhere in GOA, and the one that is apparently independent of the INO80 complex: RNAi depletion of hArp8 misaligns mitotic chromosomes, while depletion of hIno80 or hArp5 does not. Reason: GOA's nearest existing row is GO:0033044 regulation of chromosome organization, supported by an INO80-complex RNAi experiment in a different paper, and GO:0007080 is not a descendant of it - checking the QuickGO ancestor list for GO:0007080 with relations is_a,part_of gives GO:0051276 chromosome organization but not the regulation branch - so this is a genuine addition rather than a specificity upgrade of an existing row. Two independent perturbations give the phenotype, RNAi depletion and expression of truncated hArp8, and the controls are what make it ARP8-specific rather than complex-borne: depleting hIno80 or hArp5 does not misalign chromosomes, hArp5 does not accumulate on mitotic chromosomes at all, and the ARP8-ACTR5 interaction is undetectable in metaphase-arrested cells. The evidence code is IMP rather than IDA because the assay is a loss-of-function phenotype. The underlying molecular activity is unknown and is filed as a knowledge gap rather than guessed at. Supporting Evidence: PMID:18163988 Expression of truncated hArp8 proteins and depletion of endogenous hArp8 by RNA interference caused misalignment of mitotic chromosomes, suggesting that chromosome-associated hArp8 has a role in chromosome behavior. PMID:18163988 In contrast, depletion of hIno80 and hArp5 did not cause misalignment of chromosomes, suggesting that the role of hArp8 at mitotic chromosomes is independent of the activity of hINO80 complexes.
GO:0000793 condensed chromosome	IDA PMID:18163988 The actin-related protein hArp8 accumulates on the mitotic c...	NEW	Summary: hArp8 accumulates on mitotic chromosomes by immunofluorescence, the first actin family member reported to do so. Proposed as an addition to the existing general chromosome row, not as a replacement for it. Reason: GOA has GO:0005694 chromosome from the UniProt subcellular-location mapping, whose underlying statement notes that ARP8 specifically localises to mitotic chromosomes, so the specific compartment is documented but not annotated. GO:0000793 condensed chromosome is a descendant of GO:0005694 (confirmed against the QuickGO ancestor list), which is why this could have been written as a MODIFY - and it deliberately is not. ARP8 also acts on interphase chromatin: it is required for INO80 recruitment to laser-induced damage in interphase nuclei and works within INO80 during replication and transcription. Replacing the general term with the condensed-chromosome term would therefore delete the interphase association, so the general row is kept and this is added alongside it. Additive rather than corrective, because the existing call is defensible and merely incomplete. Supporting Evidence: PMID:18163988 Here we report that hArp8, but not hArp5, accumulates on mitotic chromosomes. PMID:18163988 This is the first example where a member of the actin family is found to be associated with mitotic chromosomes. file:human/ACTR8/ACTR8-uniprot.txt Note=Specifically localizes to mitotic

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