Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The proteome of Saccharomyces cerevisiae mitochondria.
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Sickmann et al. used highly purified S. cerevisiae mitochondria in a mass-spectrometry survey that underlies one of the high-throughput CBR1 mitochondrial localization rows.
"We performed a comprehensive approach to determine the proteome of Saccharomyces cerevisiae mitochondria."
Studies on the microsomal electron-transport system of anaerobically grown yeast. IV. Purification and characterization of NADH-cytochrome b5 reductase.
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The yeast microsomal enzyme was purified, contained loosely bound FAD, and used NADH as the specific electron donor for cytochrome b5 reduction.
"The reductase required NADH as a specific electron donor, and could reduce some redox dyes as well as cytochrom b5."
Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins.
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Zahedi et al. purified S. cerevisiae mitochondrial outer membranes for a compartment-focused proteomic survey that supports CBR1 mitochondrial outer-membrane localization.
"We used a eukaryotic model organism, the yeast Saccharomyces cerevisiae, to determine the proteome of highly purified mitochondrial outer membranes."
Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics.
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Reinders et al. combined multidimensional LC-MS/MS, 1D gel/nano-LC-MS/MS, and 2D gel/MALDI methods to expand the S. cerevisiae mitochondrial proteome.
"A total of 851 different proteins (PROMITO dataset) were identified by use of multidimensional LC-MS/MS, 1D-SDS-PAGE combined with nano-LC-MS/MS and 2D-PAGE with subsequent MALDI-mass fingerprinting."
Dph3 is an electron donor for Dph1-Dph2 in the first step of eukaryotic diphthamide biosynthesis.
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Dph3 was shown to be an electron donor for Dph1-Dph2, and the endogenous reductase that reduces Dph3 had not yet been identified.
"NorW was used to reduce Dph3. The identity of the endogenous reductase for Dph3 is unknown."
Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae.
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Renvoise et al. performed a quantitative proteomic and phosphoproteomic study of mitochondria isolated from yeast grown on fermentative and respiratory media.
"we performed an overall quantitative proteomic and phosphoproteomic study of isolated mitochondria extracted from yeast grown on fermentative (glucose or galactose) and respiratory (lactate) media."
One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy.
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The SWAT-GFP resource used N-terminally tagged strains and high-content microscopy to assign subcellular localizations at high throughput.
"To establish this strategy we constructed a library containing ~1,800 strains where all proteins with known or predicted localization to the yeast endomembrane system are tagged with an amino terminal"
Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification.
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Cbr1 was identified as an NADH-dependent Dph3 reductase, rapidly reduced Dph3 in vitro when NADH was supplied, and supported in vitro Dph1-Dph2 radical-SAM activity through the Cbr1/NADH/Dph3 reduction system.
"Upon addition of NADH to initiate the reaction, Dph3 was rapidly reduced by Cbr1"
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Loss of CBR1 alone partially impaired mcm5s2U tRNA wobble uridine modification, and combined loss of CBR1 and MCR1 further reduced this Dph3-dependent modification.
"CBR1 deletion alone conferred some resistance to γ-toxin, suggesting that formation of tRNA modifications was partially impaired"
The asymmetric function of Dph1-Dph2 heterodimer in diphthamide biosynthesis.
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The Dph2 Fe-S cluster helps pass reducing equivalents from the Dph3/Cbr1/NADH system to the catalytic Dph1 cluster.
"the Dph1 cluster serves a catalytic role, while the Dph2 cluster facilitates the reduction of the Dph1 cluster by the physiological reducing system Dph3/Cbr1/NADH."
Dph3 Enables Aerobic Diphthamide Biosynthesis by Donating One Iron Atom to Transform a [3Fe-4S] to a [4Fe-4S] Cluster in Dph1-Dph2.
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Dph3/Cbr1/NADH is the physiological reducing system for Dph1-Dph2, and Dph3 can donate iron to convert damaged [3Fe-4S] Dph1-Dph2 to the active [4Fe-4S] form during the radical-SAM cycle.
"Under physiological conditions, the reduction of the [4Fe–4S] clusters in Dph1–Dph2 requires Dph3 and Cbr1."
UniProt record for Saccharomyces cerevisiae CBR1
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The S. cerevisiae CBR1 Swiss-Prot record assigns P38626 to PANTHER subfamily PTHR19370:SF184, EC 1.6.2.2, and the RHEA:46680 NADH:ferricytochrome-b5 and RHEA:71231 NADH:Dph3 reductase reactions.
"PANTHER; PTHR19370:SF184; NADH-CYTOCHROME B5 REDUCTASE-LIKE"
PTHR19370 PAINT annotations
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PAINT node PTN001064671 is the CBR1-like Saccharomycetes ancestor used to propagate cytochrome-b5 reductase activity and plasma-membrane localization to S. cerevisiae CBR1.
"PTHR19370 PTN001064671 GO:0004128 F IBD false"