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SGD:YFH1

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Contents

Species (Taxon ID) Saccharomyces cerevisiae (baker's yeast) (taxon:4932)
Gene Name(s) YFH1 ( synonyms: YDL120W )
Protein Name(s) Mitochondrial matrix iron chaperone,
External Links
SGD S000002278

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0016226

iron-sulfur cluster assembly

PMID:12065597[1]

IMP: Inferred from Mutant Phenotype

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

GO:0004322

ferroxidase activity

SGD_REF:S000118616
PMID:12149269[2]

IDA: Inferred from Direct Assay

F

From SGD

GO:0004322

ferroxidase activity

SGD_REF:S000121078
PMID:12732649[3]

IDA: Inferred from Direct Assay

F

From SGD

GO:0004322

ferroxidase activity

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR017789

F

From SGD

GO:0004322

ferroxidase activity

SGD_REF:S000124037

IEA: Inferred from Electronic Annotation

EC:1.16.3.1

F

From SGD

GO:0005739

mitochondrion

SGD_REF:S000044796
PMID:9241271[4]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005739

mitochondrion

SGD_REF:S000049863
PMID:9180083[5]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005739

mitochondrion

SGD_REF:S000075100
PMID:14576278[6]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005739

mitochondrion

SGD_REF:S000117178
PMID:16823961[7]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005739

mitochondrion

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0496

C

From SGD

GO:0005759

mitochondrial matrix

SGD_REF:S000050931
PMID:10428860[8]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005759

mitochondrial matrix

SGD_REF:S000148671

IEA: Inferred from Electronic Annotation

UniProtKB-SubCell:SL-0170

C

From SGD

GO:0006749

glutathione metabolic process

SGD_REF:S000126765
PMID:18562474[9]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0006783

heme biosynthetic process

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0350

P

From SGD

GO:0006810

transport

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0813

P

From SGD

GO:0006811

ion transport

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0406

P

From SGD

GO:0006879

cellular iron ion homeostasis

SGD_REF:S000049863
PMID:9180083[5]

IDA: Inferred from Direct Assay

P

From SGD

GO:0006879

cellular iron ion homeostasis

SGD_REF:S000049863
PMID:9180083[5]

IGI: Inferred from Genetic Interaction

SGD:S000004741

P

From SGD

GO:0006879

cellular iron ion homeostasis

SGD_REF:S000049863
PMID:9180083[5]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0006879

cellular iron ion homeostasis

SGD_REF:S000069054
PMID:11734220[10]

IGI: Inferred from Genetic Interaction

P

From SGD

GO:0006879

cellular iron ion homeostasis

SGD_REF:S000069054
PMID:11734220[10]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0006879

cellular iron ion homeostasis

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0409

P

From SGD

GO:0008198

ferrous iron binding

SGD_REF:S000048112
PMID:10930361[11]

IDA: Inferred from Direct Assay

F

From SGD

GO:0008198

ferrous iron binding

SGD_REF:S000116797
PMID:16784228[12]

IDA: Inferred from Direct Assay

F

From SGD

GO:0016226

iron-sulfur cluster assembly

SGD_REF:S000068798
PMID:12970193[13]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0016226

iron-sulfur cluster assembly

SGD_REF:S000071167
PMID:12221295[14]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0016226

iron-sulfur cluster assembly

SGD_REF:S000075383
PMID:14741370[15]

IGI: Inferred from Genetic Interaction

SGD:S000006056

P

From SGD

GO:0016226

iron-sulfur cluster assembly

SGD_REF:S000075383
PMID:14741370[15]

IPI: Inferred from Physical Interaction

SGD:S000006056

P

From SGD

GO:0016226

iron-sulfur cluster assembly

SGD_REF:S000076149
PMID:12947415[16]

IDA: Inferred from Direct Assay

P

From SGD

GO:0016226

iron-sulfur cluster assembly

SGD_REF:S000076149
PMID:12947415[16]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0016491

oxidoreductase activity

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0560

F

From SGD

GO:0034986

iron chaperone activity

SGD_REF:S000117118
PMID:15247478[17]

IGI: Inferred from Genetic Interaction

UniProtKB:Q16595

F

From SGD

GO:0034986

iron chaperone activity

SGD_REF:S000121078
PMID:12732649[3]

IDA: Inferred from Direct Assay

F

From SGD

GO:0055072

iron ion homeostasis

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0410

P

From SGD

GO:0055114

oxidation-reduction process

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR017789

P

From SGD

GO:0055114

oxidation-reduction process

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0560

P

From SGD


edit table

Notes

References

See Help:References for how to manage references in GONUTS.
  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. ↑ Park S et al. (2002) The ferroxidase activity of yeast frataxin. J Biol Chem 277: 38589-95 PubMed GONUTS page
  3. ↑ 3.0 3.1 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
  4. ↑ 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
  5. ↑ 5.0 5.1 5.2 5.3 Babcock M et al. (1997) Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin. Science 276: 1709-12 PubMed GONUTS page
  6. ↑ Sickmann A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc Natl Acad Sci U S A 100: 13207-12 PubMed GONUTS page
  7. ↑ 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
  8. ↑ 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
  9. ↑ 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
  10. ↑ 10.0 10.1 Chen OS & Kaplan J (2001) YFH1-mediated iron homeostasis is independent of mitochondrial respiration. FEBS Lett 509: 131-4 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. ↑ 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
  14. ↑ 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
  15. ↑ 15.0 15.1 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
  16. ↑ 16.0 16.1 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
  17. ↑ Bulteau AL et al. (2004) Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 305: 242-5 PubMed GONUTS page
Retrieved from "http://gowiki.tamu.edu/wiki/index.php/SGD:YFH1"
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