| Evidence item (function/localization) | Species/context | Key finding | Experimental basis (brief) | Citation (first author year) | Publication date (month/year) | URL |
|---|---|---|---|---|---|---|
| Dual function in Atp6 processing and ATP synthase assembly | *Saccharomyces cerevisiae* Atp23; used as orthologous functional evidence for human ATP23/Q9Y6H3 | ATP23 encodes a conserved metalloprotease required to remove the ~10-residue N-terminal presequence from Atp6/subunit 6; protease-dead mutant still supports assembly/respiratory growth, implying a second assembly/chaperone-like role. Atp23 is associated with the inner membrane and its C-terminus faces the IMS. (pqac-00000006, pqac-00000008, pqac-00000009) | Yeast genetics, catalytic-site mutagenesis (E168Q), mitochondrial translation/assembly assays, respiratory growth rescue, biochemical topology/processing analysis | Zeng 2007 | Feb 2007 | https://doi.org/10.1091/mbc.e06-09-0801 |
| IMS localization and separable protease vs chaperone functions | *S. cerevisiae* Atp23; strongest mechanistic evidence for ATP23-family role | Atp23 localizes to the mitochondrial intermembrane space; protease-protection and alkaline extraction place the HA-tagged C-terminus in the IMS. Protease activity is required for Atp6 maturation, but protease-inactive mutants still allow assembly of functional F1FO-ATP synthase, separating Atp23's processing and chaperone/assembly roles. Genetic interaction with prohibitins links Atp23 to inner-membrane proteostasis/ATP synthase biogenesis. (pqac-00000002, pqac-00000003, pqac-00000004, pqac-00000012) | Protease protection, alkaline extraction, BN-PAGE, co-immunoprecipitation with Atp6, site-directed mutagenesis, yeast genetic interaction analysis | Osman 2007 | Feb 2007 | https://doi.org/10.1091/mbc.e06-09-0839 |
| Human ATP synthase assembly context | Human mitochondria; ATP23 discussed as yeast assembly factor context rather than directly functionally tested in human cells in the cited excerpt | Human ATP synthase membrane-domain assembly paper cites yeast ATP23/Atp23 as an assembly factor associated with ATP6/ATP8 biogenesis. The excerpt supports relevance of ATP23 to ATP synthase assembly models, but does not provide direct experimental characterization of human ATP23 in that paper excerpt. (pqac-00000005) | Human ATP synthase assembly study with citation-based contextual comparison to yeast ATP23 literature | He 2018 | Feb 2018 | https://doi.org/10.1073/pnas.1722086115 |
| Review statement: IMS protease role in ATP synthase biogenesis | Yeast/human mitochondrial biogenesis review | Review identifies Atp23 as an IMS protease required for processing Atp6 during ATP synthase biogenesis, reinforcing the submitochondrial localization and functional model derived from yeast primary studies. (pqac-00000012) | Review synthesis of prior mitochondrial biogenesis/protease literature | Geldon 2021 | Sep 2021 | https://doi.org/10.3389/fcell.2021.720656 |
| KUB3/XRCC6BP1 naming and DNA double-strand break repair claim | Human glioblastoma; same symbol/synonym space relevant to ATP23 alias ambiguity | KUB3 is explicitly described as Ku70-binding protein 3 and also termed XRCC6BP1; elevated KUB3 amplification/expression correlated with more efficient DNA double-strand break repair after ionizing radiation, and prior Ku70 binding was noted/confirmed. The paper excerpt does not mention ATP23, ENSG00000166896, or mitochondrial localization, so it should be treated cautiously as alias-linked but functionally distinct literature relative to mitochondrial ATP23 annotation. (pqac-00000010, pqac-00000011) | Glioma cell expression/amplification analyses, siRNA knockdown, ectopic expression, DSB-repair assays after irradiation, co-immunoprecipitation with Ku70 | Fischer 2013 | May 2013 | https://doi.org/10.3892/ijo.2013.1937 |
| Atp23 in mitochondrial proteolysis screen for α-synuclein toxicity | Yeast mitochondrial protease overexpression screen | Atp23 was one of the yeast mitochondrial proteases whose increased copy number reduced mitochondrial α-synuclein accumulation; Atp23 grouped with Cym1, Prd1, and Imp2 among the strongest inhibitors of α-syn accumulation and helped rescue growth and membrane-potential defects in the yeast model. This is indirect, non-human evidence linking Atp23-family activity to mitochondrial proteostasis. (pqac-00000013, pqac-00000014) | Yeast MoBY plasmid overexpression screen, α-syn spGFP quantification, immunoblotting, growth rescue, membrane-potential assays | Zhang 2024 | Jun 2024 | https://doi.org/10.1038/s41531-024-00733-y |


*Table: This table compiles the most relevant evidence for annotating human ATP23/Q9Y6H3, separating direct human alias literature from stronger mechanistic ortholog evidence in yeast. It is useful for clarifying localization, catalytic/assembly roles, and naming ambiguity involving KUB3/XRCC6BP1.*