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

Last Reviewed on: 2008-08-11    Molecular Function | Biological Process | Cellular Component

Manually curated Molecular Function
Annotation(s)	Evidence	Reference(s)	Assigned By
ATPase activity	IDA: Inferred from Direct Assay Assigned on 2008-07-17	Dubaquie Y, et al.  (1997) Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60. Proc Natl Acad Sci U S A 94(17):9011-6	SGD
	IDA: Inferred from Direct Assay Assigned on 2008-07-16	Rospert S, et al.  (1993) Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria. Proc Natl Acad Sci U S A 90(23):10967-71	SGD
chaperone binding	IPI: Inferred from Physical Interaction with SGD:HSP10 Assigned on 2008-08-11	Dubaquie Y, et al.  (1997) Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60. Proc Natl Acad Sci U S A 94(17):9011-6	SGD
DNA replication origin binding	IDA: Inferred from Direct Assay Assigned on 2008-07-18	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
single-stranded DNA binding	IDA: Inferred from Direct Assay Assigned on 2004-07-16	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
unfolded protein binding	IMP: Inferred from Mutant Phenotype Assigned on 2008-07-16	Martin J, et al.  (1992) Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science 258(5084):995-8	SGD

Manually curated Biological Process
Annotation(s)	Evidence	Reference(s)	Assigned By
'de novo' protein folding	IMP: Inferred from Mutant Phenotype Assigned on 2008-07-15	Cheng MY, et al.  (1990) The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348(6300):455-8	SGD
chaperone-mediated protein complex assembly	IMP: Inferred from Mutant Phenotype Assigned on 2008-07-15	Cheng MY, et al.  (1989) Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337(6208):620-5	SGD
protein import into mitochondrial intermembrane space	IMP: Inferred from Mutant Phenotype Assigned on 2008-07-16	Koll H, et al.  (1992) Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 68(6):1163-75	SGD
protein maturation	IMP: Inferred from Mutant Phenotype Assigned on 2008-07-16	Hallberg EM, et al.  (1993) Loss of mitochondrial hsp60 function: nonequivalent effects on matrix-targeted and intermembrane-targeted proteins. Mol Cell Biol 13(5):3050-7	SGD
protein refolding	IMP: Inferred from Mutant Phenotype Assigned on 2008-07-16	Martin J, et al.  (1992) Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science 258(5084):995-8	SGD
	IDA: Inferred from Direct Assay Assigned on 2008-07-17	Dubaquie Y, et al.  (1997) Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60. Proc Natl Acad Sci U S A 94(17):9011-6	SGD
protein stabilization	IMP: Inferred from Mutant Phenotype Assigned on 2008-07-16	Martin J, et al.  (1992) Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science 258(5084):995-8	SGD

Manually curated Cellular Component
Annotation(s)	Evidence	Reference(s)	Assigned By
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
mitochondrion	IDA: Inferred from Direct Assay Assigned on 2009-07-01	Grandier-Vazeille X, et al.  (2001) Yeast mitochondrial dehydrogenases are associated in a supramolecular complex. Biochemistry 40(33):9758-69	SGD
	IDA: Inferred from Direct Assay Assigned on 2001-01-18	Hallberg EM, et al.  (1993) Loss of mitochondrial hsp60 function: nonequivalent effects on matrix-targeted and intermembrane-targeted proteins. Mol Cell Biol 13(5):3050-7	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
	IDA: Inferred from Direct Assay Assigned on 2004-09-24	Sickmann A, et al.  (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc Natl Acad Sci U S A 100(23):13207-12	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
ATP binding	IEA: Inferred from Electronic Annotation with EBI:IPR002423, EBI:IPR018370 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-0067 Last updated 2013-03-02	UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries.	UniProtKB
nucleotide binding	IEA: Inferred from Electronic Annotation with EBI:KW-0547 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 Biological Process
Annotation(s)	Evidence	Reference(s)	Assigned By
cellular protein metabolic process	IEA: Inferred from Electronic Annotation with EBI:IPR002423 Last updated 2013-03-02	DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms.	InterPro
protein folding	IEA: Inferred from Electronic Annotation with EBI:IPR018370 Last updated 2013-03-02	DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms.	InterPro
protein refolding	IEA: Inferred from Electronic Annotation with EBI:IPR001844 Last updated 2013-03-02	DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms.	InterPro
response to stress	IEA: Inferred from Electronic Annotation with EBI:KW-0346 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:IPR018370, EBI:IPR001844 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)).