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YEAST:FRDA

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) YFH1
Protein Name(s) Frataxin homolog, mitochondrial

Frataxin homolog intermediate form

External Links
UniProt Q07540
EMBL Z74168
AY558160
BK006938
PIR S67663
RefSeq NP_010163.1
PDB 2FQL
2GA5
3OEQ
3OER
4EC2
PDBsum 2FQL
2GA5
3OEQ
3OER
4EC2
ProteinModelPortal Q07540
SMR Q07540
BioGrid 31943
DIP DIP-7485N
IntAct Q07540
MINT MINT-4300743
STRING 4932.YDL120W
MaxQB Q07540
PaxDb Q07540
EnsemblFungi [example_ID YDL120W]
GeneID 851437
KEGG sce:YDL120W
CYGD YDL120w
SGD S000002278
eggNOG COG1965
GeneTree ENSGT00390000005811
HOGENOM HOG000190729
InParanoid Q07540
OMA HIPEVEY
OrthoDB EOG7WDNF7
BioCyc MetaCyc:G3O-29519-MONOMER
YEAST:G3O-29519-MONOMER
Reactome REACT_189012
REACT_189017
EvolutionaryTrace Q07540
NextBio 968672
PRO PR:Q07540
Proteomes UP000002311
Genevestigator Q07540
GO GO:0005743
GO:0005758
GO:0005759
GO:0005739
GO:0008199
GO:0008198
GO:0004322
GO:0034986
GO:0006879
GO:0006749
GO:0006783
GO:0006811
GO:0016226
GO:0006121
GO:0010040
GO:0006979
Gene3D 3.30.920.10
InterPro IPR017789
IPR002908
IPR020895
PANTHER PTHR16821
Pfam PF01491
SUPFAM SSF55387
TIGRFAMs TIGR03421
TIGR03422
PROSITE PS01344
PS50810

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0016226

iron-sulfur cluster assembly

PMID:12065597[1]

ECO:0000315

P

Figure 5 (A) and 5 (B). yfh1 deletion clearly has resulted decrease number of Fe/S protein maturation in mitochondria compared to the wildtype.

complete
CACAO 4904

part_of

GO:0005739

mitochondrion

PMID:16823961[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:24769239[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:14576278[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0016226

iron-sulfur cluster assembly

PMID:12065597[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0034986

iron chaperone activity

PMID:15247478[5]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:Q16595

F

Seeded From UniProt

complete

enables

GO:0034986

iron chaperone activity

PMID:12732649[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0016226

iron-sulfur cluster assembly

PMID:14741370[7]

ECO:0000353

physical interaction evidence used in manual assertion

SGD:S000006056

P

Seeded From UniProt

complete

involved_in

GO:0016226

iron-sulfur cluster assembly

PMID:14741370[7]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000006056

P

Seeded From UniProt

complete

involved_in

GO:0016226

iron-sulfur cluster assembly

PMID:12221295[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016226

iron-sulfur cluster assembly

PMID:12947415[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016226

iron-sulfur cluster assembly

PMID:12970193[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016226

iron-sulfur cluster assembly

PMID:12947415[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008198

ferrous iron binding

PMID:10930361[11]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008198

ferrous iron binding

PMID:16784228[12]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006879

cellular iron ion homeostasis

PMID:9180083[13]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000004741

P

Seeded From UniProt

complete

involved_in

GO:0006879

cellular iron ion homeostasis

PMID:11734220[14]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P35999

P

Seeded From UniProt

complete

involved_in

GO:0006879

cellular iron ion homeostasis

PMID:11734220[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006879

cellular iron ion homeostasis

PMID:9180083[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006879

cellular iron ion homeostasis

PMID:9180083[13]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006749

glutathione metabolic process

PMID:18562474[15]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005759

mitochondrial matrix

PMID:10428860[16]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:9241271[17]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:9180083[13]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004322

ferroxidase activity

PMID:12149269[18]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004322

ferroxidase activity

PMID:12732649[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0010040

response to iron(II) ion

PMID:16371422[19]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006979

response to oxidative stress

PMID:16371422[19]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006121

mitochondrial electron transport, succinate to ubiquinone

PMID:15961414[20]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051537

2 iron, 2 sulfur cluster binding

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000423706
UniProtKB:Q16595

F

Seeded From UniProt

complete

enables

GO:0034986

iron chaperone activity

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0030092
PANTHER:PTN000423706
SGD:S000002278
UniProtKB:Q16595

F

Seeded From UniProt

complete

involved_in

GO:0018283

iron incorporation into metallo-sulfur cluster

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000423706
UniProtKB:Q16595

P

Seeded From UniProt

complete

enables

GO:0008199

ferric iron binding

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000423706
UniProtKB:Q16595

F

Seeded From UniProt

complete

enables

GO:0008198

ferrous iron binding

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000423706
SGD:S000002278
UniProtKB:Q16595

F

Seeded From UniProt

complete

involved_in

GO:0007005

mitochondrion organization

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1096879
PANTHER:PTN000423706

P

Seeded From UniProt

complete

involved_in

GO:0006879

cellular iron ion homeostasis

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1096879
PANTHER:PTN000423706
SGD:S000002278
UniProtKB:Q16595

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0030092
MGI:MGI:1096879
PANTHER:PTN000423706
PomBase:SPCC1183.03c
RGD:1565754
SGD:S000002278
TAIR:locus:2125477
UniProtKB:Q16595
WB:WBGene00001486

C

Seeded From UniProt

complete

enables

GO:0004322

ferroxidase activity

PMID:21873635[21]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000423706
SGD:S000002278
UniProtKB:Q16595

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:17027502[22]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q07540

F

Seeded From UniProt

complete

enables

GO:0004322

ferroxidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017789

F

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017789

C

Seeded From UniProt

complete

enables

GO:0008199

ferric iron binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002908
InterPro:IPR036524

F

Seeded From UniProt

complete

involved_in

GO:0016226

iron-sulfur cluster assembly

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002908
InterPro:IPR036524

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017789

P

Seeded From UniProt

complete

enables

GO:0004322

ferroxidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.16.3.1

F

Seeded From UniProt

complete

part_of

GO:0005759

mitochondrial matrix

Reactome:R-SCE-1252253

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005758

mitochondrial intermembrane space

Reactome:R-SCE-1268014

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005743

mitochondrial inner membrane

Reactome:R-SCE-1268017
Reactome:R-SCE-1268014
Reactome:R-SCE-1252253

ECO:0000304

author statement supported by traceable reference used in manual assertion



C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

involved_in

GO:0006811

ion transport

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0406

P

Seeded From UniProt

complete

involved_in

GO:0006783

heme biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0350

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496

C

Seeded From UniProt

complete

involved_in

GO:0006879

cellular iron ion homeostasis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0409

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0055072

iron ion homeostasis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0410

P

Seeded From UniProt

complete

part_of

GO:0005759

mitochondrial matrix

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0170

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 Mühlenhoff, U et al. (2002) Characterization of iron-sulfur protein assembly in isolated mitochondria. A requirement for ATP, NADH, and reduced iron. J. Biol. Chem. 277 29810-6 PubMed GONUTS page
  2. ↑ Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
  3. ↑ Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 PubMed GONUTS page
  4. ↑ Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page
  5. ↑ Bulteau, AL et al. (2004) Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 305 242-5 PubMed GONUTS page
  6. ↑ 6.0 6.1 Park, S et al. (2003) Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation. J. Biol. Chem. 278 31340-51 PubMed GONUTS page
  7. ↑ 7.0 7.1 Ramazzotti, A et al. (2004) Mitochondrial functional interactions between frataxin and Isu1p, the iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae. FEBS Lett. 557 215-20 PubMed GONUTS page
  8. ↑ Chen, OS et al. (2002) Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: evidence that Yfh1p affects Fe-S cluster synthesis. Proc. Natl. Acad. Sci. U.S.A. 99 12321-6 PubMed GONUTS page
  9. ↑ 9.0 9.1 Gerber, J et al. (2003) An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep. 4 906-11 PubMed GONUTS page
  10. ↑ Mühlenhoff, U et al. (2003) Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 22 4815-25 PubMed GONUTS page
  11. ↑ Adamec, J et al. (2000) Iron-dependent self-assembly of recombinant yeast frataxin: implications for Friedreich ataxia. Am. J. Hum. Genet. 67 549-62 PubMed GONUTS page
  12. ↑ Cook, JD et al. (2006) Monomeric yeast frataxin is an iron-binding protein. Biochemistry 45 7767-77 PubMed GONUTS page
  13. ↑ 13.0 13.1 13.2 13.3 Babcock, M et al. (1997) Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin. Science 276 1709-12 PubMed GONUTS page
  14. ↑ 14.0 14.1 Chen, OS & Kaplan, J (2001) YFH1-mediated iron homeostasis is independent of mitochondrial respiration. FEBS Lett. 509 131-4 PubMed GONUTS page
  15. ↑ Auchère, F et al. (2008) Glutathione-dependent redox status of frataxin-deficient cells in a yeast model of Friedreich's ataxia. Hum. Mol. Genet. 17 2790-802 PubMed GONUTS page
  16. ↑ Branda, SS et al. (1999) Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidase. J. Biol. Chem. 274 22763-9 PubMed GONUTS page
  17. ↑ Wilson, RB & Roof, DM (1997) Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue. Nat. Genet. 16 352-7 PubMed GONUTS page
  18. ↑ Park, S et al. (2002) The ferroxidase activity of yeast frataxin. J. Biol. Chem. 277 38589-95 PubMed GONUTS page
  19. ↑ 19.0 19.1 Gakh, O et al. (2006) Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity. Hum. Mol. Genet. 15 467-79 PubMed GONUTS page
  20. ↑ González-Cabo, P et al. (2005) Frataxin interacts functionally with mitochondrial electron transport chain proteins. Hum. Mol. Genet. 14 2091-8 PubMed GONUTS page
  21. ↑ 21.0 21.1 21.2 21.3 21.4 21.5 21.6 21.7 21.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  22. ↑ Karlberg, T et al. (2006) The structures of frataxin oligomers reveal the mechanism for the delivery and detoxification of iron. Structure 14 1535-46 PubMed GONUTS page
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