Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on curation of immunofluorescence data
cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs.
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ABCF2 was identified in a cloning study of mRNAs responsive to cellular iron levels, but this does not establish a GO process or transporter function.
"We tested this new method on eight mRNAs that we have previously shown to respond to cellular iron levels."
Identification of overexpression and amplification of ABCF2 in clear cell ovarian adenocarcinomas by cDNA microarray analyses.
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ABCF2 copy number and expression are elevated in ovarian clear cell adenocarcinoma relative to serous cases, and cytoplasmic staining was higher in chemotherapy nonresponders.
"The results showed significantly higher ABCF2 DNA and mRNA copy number and protein levels in clear cell cases compared with those in serous cases."
Defining the membrane proteome of NK cells.
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The high-throughput NK-cell membrane-proteome study identified many nonintegral or transiently membrane-associated proteins, making the broad ABCF2 membrane row weak.
"The remaining species were largely involved in cellular processes and molecular functions that could be predicted to be transiently associated with membranes."
ABCF2, an Nrf2 target gene, contributes to cisplatin resistance in ovarian cancer cells.
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ABCF2 is a cytosolic ABCF protein with nucleotide-binding domains but no transmembrane domains, distinguishing it from membrane transporters.
"ABCF2 possesses nucleotide-binding domains, but has no transmembrane domains, which makes it different from other members of the ATP binding cassette family since it cannot function as a membrane transporter"
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NFE2L2/NRF2 regulates ABCF2 expression through a functional promoter ARE in ovarian cancer cells.
"To further confirm that NRF2 binds to the putative ARE of the ABCF2 promoter, a CHIP assay was performed in A2780cp cells."
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Manipulating ABCF2 abundance changes cisplatin response in ovarian cancer cell-line assays, but the mechanism remains unresolved.
"ABCF2 overexpression rendered A2780 cells more resistant to cisplatin and ABCF2 knockdown rendered resistant A2780 cells more sensitive to cisplatin"
Enteropathogenic Escherichia coli effector EspF interacts with host protein Abcf2.
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ABCF2 (Abcf2) was identified by affinity purification as a binding partner of the enteropathogenic E. coli (EPEC) type III effector EspF, with the interaction confirmed by yeast two-hybrid, colocalization, and co-immunoprecipitation from infected cells. This is direct experimental evidence for an ABCF2 protein-protein interaction, surfaced by the Falcon deep research report.
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EPEC infection decreased ABCF2 levels in an EspF dose-dependent manner, and RNAi knockdown of ABCF2 increased EspF-induced caspase-9 and caspase-3 cleavage and increased staurosporine-induced caspase-3 cleavage, indicating a putative anti-apoptotic (cytoprotective) function for ABCF2 that EspF antagonizes via the intrinsic/mitochondrial death pathway.
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ABCF2 was described as primarily cytoplasmic with partial mitochondrial localization in this study; this is consistent with influence on mitochondrial apoptosis but does not by itself justify a stable mitochondrial GO localization annotation without further evidence.
NFE2L2 dependent ABCF2 expression
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Reactome models ABCF2 as an NFE2L2 target gene with evidence from Bao et al. 2017; this supports transcriptional-regulation context, not plasma membrane localization.
"ABCF2 is an NFE2L2 target gene that contains a functional ARE sequence in the promoter which is confirmed through ChIP assay in Human Ovarian cancer cell lines."
UniProt record for ABCF2
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UniProt annotates ABCF2 as an ABCF-family protein with two ABC transporter domains, two ATP-binding sites, and no transmembrane-domain transporter role.
"Lacks transmembrane domains and is probably not involved in transport."
Manual notes for ABCF2 Proteostasis PN review