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

Last Reviewed on: 2006-06-13    Molecular Function | Biological Process

Manually curated Molecular Function
Annotation(s)	Evidence	Reference(s)	Assigned By
ATPase activity	IDA: Inferred from Direct Assay Assigned on 2011-03-16	Cunningham CN, et al.  (2008) Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90. J Biol Chem 283(30):21170-8	SGD
ATPase activity, coupled	ISS: Inferred from Sequence or structural Similarity with SGD:HSP82 Assigned on 2006-06-13	Borkovich KA, et al.  (1989) hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol Cell Biol 9(9):3919-30	SGD
unfolded protein binding	IDA: Inferred from Direct Assay Assigned on 2006-06-13	Scheibel T, et al.  (1998) Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. Proc Natl Acad Sci U S A 95(4):1495-9	SGD

Manually curated Biological Process
Annotation(s)	Evidence	Reference(s)	Assigned By
'de novo' protein folding	ISS: Inferred from Sequence or structural Similarity with SGD:HSP82 Assigned on 2006-06-13	Borkovich KA, et al.  (1989) hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol Cell Biol 9(9):3919-30	SGD
box C/D snoRNP assembly	IMP: Inferred from Mutant Phenotype Assigned on 2012-03-06	Zhao R, et al.  (2008) Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J Cell Biol 180(3):563-78	SGD
proteasome assembly	IMP: Inferred from Mutant Phenotype Assigned on 2005-01-11 IPI: Inferred from Physical Interaction Assigned on 2005-01-11	Imai J, et al.  (2003) The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J 22(14):3557-67	SGD
protein folding	IMP: Inferred from Mutant Phenotype Assigned on 2001-01-18	Nathan DF and Lindquist S  (1995) Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol Cell Biol 15(7):3917-25	SGD
protein refolding	ISS: Inferred from Sequence or structural Similarity with SGD:HSP82 Assigned on 2006-06-13	Borkovich KA, et al.  (1989) hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol Cell Biol 9(9):3919-30	SGD
response to stress	IMP: Inferred from Mutant Phenotype Assigned on 2001-01-18	Borkovich KA, et al.  (1989) hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol Cell Biol 9(9):3919-30	SGD
telomere maintenance	IMP: Inferred from Mutant Phenotype Assigned on 2007-12-11	Toogun OA, et al.  (2008) The hsp90 molecular chaperone modulates multiple telomerase activities. Mol Cell Biol 28(1):457-67	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
cytoplasm	IDA: Inferred from Direct Assay Assigned on 2003-10-28	Huh WK, et al.  (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91	SGD
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 2003-12-10	Sickmann A, et al.  (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc Natl Acad Sci U S A 100(23):13207-12	SGD
plasma membrane	IDA: Inferred from Direct Assay Assigned on 2009-04-29	Delom F, et al.  (2006) The plasma membrane proteome of Saccharomyces cerevisiae and its response to the antifungal calcofluor. Proteomics 6(10):3029-39	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:IPR001404, EBI:IPR019805, EBI:IPR003594 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
unfolded protein binding	IEA: Inferred from Electronic Annotation with EBI:IPR001404, EBI:IPR019805 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
protein folding	IEA: Inferred from Electronic Annotation with EBI:IPR001404, EBI:IPR019805 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:IPR001404, EBI:IPR019805 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-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:SL-0086 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
	IEA: Inferred from Electronic Annotation with EBI:KW-0963 Last updated 2013-03-02	UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries.	UniProtKB
mitochondrion	IEA: Inferred from Electronic Annotation with EBI:SL-0173 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
	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)).