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SGD:YTA12

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Contents

Species (Taxon ID) Saccharomyces cerevisiae (baker's yeast) (taxon:4932)
Gene Name(s) YTA12 ( synonyms: YMR089C, RCA1 )
Protein Name(s) Component of the mitochondrial inner membrane m-AAA protease,
External Links
SGD S000004695

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000166

nucleotide binding

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR003593

F

From SGD

GO:0000166

nucleotide binding

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0547

F

From SGD

GO:0004222

metalloendopeptidase activity

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR011546
InterPro:IPR000642

F

From SGD

GO:0005515

protein binding

SGD_REF:S000134962
PMID:19748354[1]

IPI: Inferred from Physical Interaction

SGD:S000000819

F

From SGD

GO:0005524

ATP binding

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR000642
InterPro:IPR011546

F

From SGD

GO:0005524

ATP binding

SGD_REF:S000134962
PMID:19748354[1]

IDA: Inferred from Direct Assay

F

From SGD

GO:0005524

ATP binding

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0067

F

From SGD

GO:0005737

cytoplasm

SGD_REF:S000069459
PMID:11914276[2]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005739

mitochondrion

SGD_REF:S000069459
PMID:11914276[2]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005739

mitochondrion

SGD_REF:S000075100
PMID:14576278[3]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005739

mitochondrion

SGD_REF:S000117178
PMID:16823961[4]

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:0005743

mitochondrial inner membrane

SGD_REF:S000039413
PMID:7929327[5]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005745

m-AAA complex

SGD_REF:S000055187
PMID:8681382[6]

IDA: Inferred from Direct Assay

C

From SGD

GO:0006461

protein complex assembly

SGD_REF:S000055187
PMID:8681382[6]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0006465

signal peptide processing

SGD_REF:S000071826
PMID:12417197[7]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0006508

proteolysis

SGD_REF:S000055187
PMID:8681382[6]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0006508

proteolysis

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR000642

P

From SGD

GO:0006508

proteolysis

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0645

P

From SGD

GO:0008233

peptidase activity

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0645

F

From SGD

GO:0008237

metallopeptidase activity

SGD_REF:S000055187
PMID:8681382[6]

IMP: Inferred from Mutant Phenotype

F

From SGD

GO:0008237

metallopeptidase activity

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0482

F

From SGD

GO:0008270

zinc ion binding

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR011546

F

From SGD

GO:0016020

membrane

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR005936

C

From SGD

GO:0016020

membrane

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0472

C

From SGD

GO:0016021

integral to membrane

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR011546

C

From SGD

GO:0016021

integral to membrane

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0812

C

From SGD

GO:0016787

hydrolase activity

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0378

F

From SGD

GO:0016887

ATPase activity

SGD_REF:S000039413
PMID:7929327[5]

ISS: Inferred from Sequence or Structural Similarity

F

From SGD

GO:0016887

ATPase activity

SGD_REF:S000134962
PMID:19748354[1]

IDA: Inferred from Direct Assay

F

From SGD

GO:0016887

ATPase activity

SGD_REF:S000134962
PMID:19748354[1]

IMP: Inferred from Mutant Phenotype

F

From SGD

GO:0017111

nucleoside-triphosphatase activity

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR003593

F

From SGD

GO:0030163

protein catabolic process

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR005936

P

From SGD

GO:0031966

mitochondrial membrane

SGD_REF:S000148671

IEA: Inferred from Electronic Annotation

UniProtKB-SubCell:SL-0171

C

From SGD

GO:0045041

protein import into mitochondrial intermembrane space

SGD_REF:S000071826
PMID:12417197[7]

TAS: Traceable Author Statement

P

From SGD

GO:0046872

metal ion binding

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0479

F

From SGD

GO:0097002

mitochondrial inner boundary membrane

SGD_REF:S000128411
PMID:19019989[8]

IDA: Inferred from Direct Assay

C

From SGD


Notes

References

See Help:References for how to manage references in GONUTS.
  1. 1.0 1.1 1.2 1.3 Augustin S et al. (2009) An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases. Mol Cell 35: 574-85 PubMed GONUTS page
  2. 2.0 2.1 Kumar A et al. (2002) Subcellular localization of the yeast proteome. Genes Dev 16: 707-19 PubMed GONUTS page
  3. Sickmann A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc Natl Acad Sci U S A 100: 13207-12 PubMed GONUTS page
  4. 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
  5. 5.0 5.1 Tzagoloff A et al. (1994) A new member of a family of ATPases is essential for assembly of mitochondrial respiratory chain and ATP synthetase complexes in Saccharomyces cerevisiae. J Biol Chem 269: 26144-51 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 Arlt H et al. (1996) The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria. Cell 85: 875-85 PubMed GONUTS page
  7. 7.0 7.1 Esser K et al. (2002) A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1. J Mol Biol 323: 835-43 PubMed GONUTS page
  8. Suppanz IE et al. (2009) The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria. Mol Biol Cell 20: 572-80 PubMed GONUTS page
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