This page displays GO annotations in different sections according to the annotation method used to add that annotation to SGD.

Last Reviewed on: 2009-05-13    Molecular Function | Biological Process | Cellular Component

Manually curated Molecular Function
Annotation(s)	Evidence	Reference(s)	Assigned By
dihydrolipoyl dehydrogenase activity	IDA: Inferred from Direct Assay Assigned on 2001-01-18	Roy DJ and Dawes IW  (1987) Cloning and characterization of the gene encoding lipoamide dehydrogenase in Saccharomyces cerevisiae. J Gen Microbiol 133(4):925-33	SGD
glycine dehydrogenase (decarboxylating) activity	IMP: Inferred from Mutant Phenotype Assigned on 2008-03-21	Sinclair DA and Dawes IW  (1995) Genetics of the synthesis of serine from glycine and the utilization of glycine as sole nitrogen source by Saccharomyces cerevisiae. Genetics 140(4):1213-22	SGD
oxoglutarate dehydrogenase (succinyl-transferring) activity	IMP: Inferred from Mutant Phenotype Assigned on 2008-03-21	Dickinson JR, et al.  (1986) A mutation affecting lipoamide dehydrogenase, pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase activities in Saccharomyces cerevisiae. Mol Gen Genet 204(1):103-7	SGD
pyruvate dehydrogenase activity	IMP: Inferred from Mutant Phenotype Assigned on 2008-03-21	Dickinson JR, et al.  (1986) A mutation affecting lipoamide dehydrogenase, pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase activities in Saccharomyces cerevisiae. Mol Gen Genet 204(1):103-7	SGD

Manually curated Biological Process
Annotation(s)	Evidence	Reference(s)	Assigned By
2-oxoglutarate metabolic process	IMP: Inferred from Mutant Phenotype Assigned on 2008-03-28	Dickinson JR, et al.  (1986) A mutation affecting lipoamide dehydrogenase, pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase activities in Saccharomyces cerevisiae. Mol Gen Genet 204(1):103-7	SGD
glycine catabolic process	IMP: Inferred from Mutant Phenotype Assigned on 2001-01-18	Sinclair DA and Dawes IW  (1995) Genetics of the synthesis of serine from glycine and the utilization of glycine as sole nitrogen source by Saccharomyces cerevisiae. Genetics 140(4):1213-22	SGD
hydrogen peroxide metabolic process	IGI: Inferred from Genetic Interaction with SGD:NPT1, SGD:BNA6 Assigned on 2008-03-07 IMP: Inferred from Mutant Phenotype Assigned on 2008-03-07	Tahara EB, et al.  (2007) Dihydrolipoyl dehydrogenase as a source of reactive oxygen species inhibited by caloric restriction and involved in Saccharomyces cerevisiae aging. FASEB J 21(1):274-83	SGD
isoleucine catabolic process	IMP: Inferred from Mutant Phenotype Assigned on 2001-01-18	Dickinson JR and Dawes IW  (1992) The catabolism of branched-chain amino acids occurs via 2-oxoacid dehydrogenase in Saccharomyces cerevisiae. J Gen Microbiol 138(10):2029-33	SGD
L-serine biosynthetic process	IMP: Inferred from Mutant Phenotype Assigned on 2001-01-18	Sinclair DA and Dawes IW  (1995) Genetics of the synthesis of serine from glycine and the utilization of glycine as sole nitrogen source by Saccharomyces cerevisiae. Genetics 140(4):1213-22	SGD
leucine catabolic process	IMP: Inferred from Mutant Phenotype Assigned on 2001-01-18	Dickinson JR and Dawes IW  (1992) The catabolism of branched-chain amino acids occurs via 2-oxoacid dehydrogenase in Saccharomyces cerevisiae. J Gen Microbiol 138(10):2029-33	SGD
pyruvate metabolic process	IMP: Inferred from Mutant Phenotype Assigned on 2008-03-28	Dickinson JR, et al.  (1986) A mutation affecting lipoamide dehydrogenase, pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase activities in Saccharomyces cerevisiae. Mol Gen Genet 204(1):103-7	SGD
valine catabolic process	IMP: Inferred from Mutant Phenotype Assigned on 2001-01-18	Dickinson JR and Dawes IW  (1992) The catabolism of branched-chain amino acids occurs via 2-oxoacid dehydrogenase in Saccharomyces cerevisiae. J Gen Microbiol 138(10):2029-33	SGD

Manually curated Cellular Component
Annotation(s)	Evidence	Reference(s)	Assigned By
glycine cleavage complex	IMP: Inferred from Mutant Phenotype Assigned on 2008-03-18	Sinclair DA and Dawes IW  (1995) Genetics of the synthesis of serine from glycine and the utilization of glycine as sole nitrogen source by Saccharomyces cerevisiae. Genetics 140(4):1213-22	SGD
mitochondrial nucleoid	IDA: Inferred from Direct Assay Assigned on 2005-04-01	Kaufman BA, et al.  (2000) In organello formaldehyde crosslinking of proteins to mtDNA: identification of bifunctional proteins. Proc Natl Acad Sci U S A 97(14):7772-7	SGD
	IDA: Inferred from Direct Assay Assigned on 2003-12-18	Sato H, et al.  (2002) Identification of the YMN-1 antigen protein and biochemical analyses of protein components in the mitochondrial nucleoid fraction of the yeast Saccharomyces cerevisiae. Protoplasma 219(1-2):51-8	SGD
mitochondrial oxoglutarate dehydrogenase complex	IDA: Inferred from Direct Assay Assigned on 2004-12-07	Repetto B and Tzagoloff A  (1991) In vivo assembly of yeast mitochondrial alpha-ketoglutarate dehydrogenase complex. Mol Cell Biol 11(8):3931-9	SGD

* Manually curated GO annotations reflect our best understanding of the basic molecular function, biological process, and cellular component for this gene product. Manually curated annotations are assigned by SGD curators based on published papers when available, or by curatorial statements if necessary. Curators periodically review all Manually curated GO annotations for accuracy and completeness. The "Last Reviewed on:" date at the top of this section indicates when these annotations were last reviewed.

Cellular Component

High-throughput Cellular Component
Annotation(s)	Evidence	Reference(s)	Assigned By
mitochondrion	IDA: Inferred from Direct Assay Assigned on 2006-12-12	Reinders J, et al.  (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res 5(7):1543-54	SGD

** GO annotations from High-throughput experiments are made based on a variety of large scale high-throughput experiments, including genome-wide experiments. Many of these annotations are made based on GO annotations (or mappings to GO annotations) assigned by the authors, rather than SGD curators. While SGD curators read these publications and often work closely with authors to incorporate the information, each individual annotation may not necessarily be reviewed by a curator. GO Annotations from high-throughput experiments will be assigned only when this type of data is available, and thus may not be assigned in all three aspects of the Gene Ontologies.

Molecular Function | Biological Process | Cellular Component

Computational Molecular Function
Annotation(s)	Evidence	Reference(s)	Assigned By
dihydrolipoyl dehydrogenase activity	IEA: Inferred from Electronic Annotation with EBI:IPR006258 Last updated 2013-03-02	DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms.	InterPro
	IEA: Inferred from Electronic Annotation with IUBMB:1.8.1.4 Last updated 2013-03-02	GOA curators and MGI curators  (2001) Gene Ontology annotation based on Enzyme Commission mapping.	UniProtKB
flavin adenine dinucleotide binding	IEA: Inferred from Electronic Annotation with EBI:IPR016156, EBI:IPR006258, EBI:IPR001327, EBI:IPR004099 Last updated 2013-03-02	DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms.	InterPro
oxidoreductase activity	IEA: Inferred from Electronic Annotation with EBI:IPR016156, EBI:IPR001327, EBI:IPR004099, EBI:IPR023753 Last updated 2013-03-02	DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms.	InterPro
	IEA: Inferred from Electronic Annotation with EBI:KW-0560 Last updated 2013-03-02	UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries.	UniProtKB
oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor	IEA: Inferred from Electronic Annotation with EBI:IPR012999 Last updated 2013-03-02	DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms.	InterPro

Computational Biological Process
Annotation(s)	Evidence	Reference(s)	Assigned By
cell redox homeostasis	IEA: Inferred from Electronic Annotation with EBI:IPR004099 Last updated 2013-03-02	DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms.	InterPro
oxidation-reduction process	IEA: Inferred from Electronic Annotation with EBI:IPR016156, EBI:IPR013027, EBI:IPR006258, EBI:IPR012999, EBI:IPR001327, EBI:IPR004099, EBI:IPR023753 Last updated 2013-03-02	DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms.	InterPro
	IEA: Inferred from Electronic Annotation with EBI:KW-0560 Last updated 2013-03-02	UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries.	UniProtKB

Computational Cellular Component
Annotation(s)	Evidence	Reference(s)	Assigned By
cytoplasm	IEA: Inferred from Electronic Annotation with EBI:IPR004099 Last updated 2013-03-02	DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms.	InterPro
mitochondrial matrix	IEA: Inferred from Electronic Annotation with EBI:SL-0170 Last updated 2013-03-02	UniProt-GOA  (2011) Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries.	UniProtKB
mitochondrion	IEA: Inferred from Electronic Annotation with EBI:KW-0496 Last updated 2013-03-02	UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries.	UniProtKB

*** Computational GO Annotations are predictions. These annotations are NOT reviewed by a curator. Currently, all computational GO annotations for S. cerevisiae are assigned by an external source (for example, the Gene Ontology Annotation (GOA) project of the European Bioinformatics Institute (EBI)).