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

Last Reviewed on: 2009-02-23    Molecular Function | Biological Process | Cellular Component

Manually curated Molecular Function
Annotation(s)	Evidence	Reference(s)	Assigned By
ADP binding	IMP: Inferred from Mutant Phenotype Assigned on 2009-02-13	Hattendorf DA and Lindquist SL  (2002) Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding. Proc Natl Acad Sci U S A 99(5):2732-7	SGD
ATP binding	IMP: Inferred from Mutant Phenotype Assigned on 2009-02-13	Hattendorf DA and Lindquist SL  (2002) Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding. Proc Natl Acad Sci U S A 99(5):2732-7	SGD
ATPase activity, coupled	IMP: Inferred from Mutant Phenotype Assigned on 2009-02-13 IDA: Inferred from Direct Assay Assigned on 2009-02-13	Bosl B, et al.  (2005) Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides. J Biol Chem 280(46):38170-6	SGD
	IMP: Inferred from Mutant Phenotype Assigned on 2009-02-13	Glover JR and Lindquist S  (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94(1):73-82	SGD
chaperone binding	IDA: Inferred from Direct Assay Assigned on 2004-07-21	Glover JR and Lindquist S  (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94(1):73-82	SGD
unfolded protein binding	IDA: Inferred from Direct Assay Assigned on 2009-02-13	Bosl B, et al.  (2005) Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides. J Biol Chem 280(46):38170-6	SGD

Manually curated Biological Process
Annotation(s)	Evidence	Reference(s)	Assigned By
cellular heat acclimation	IMP: Inferred from Mutant Phenotype Assigned on 2009-02-23	Sanchez Y and Lindquist SL  (1990) HSP104 required for induced thermotolerance. Science 248(4959):1112-5	SGD
chaperone cofactor-dependent protein refolding	IDA: Inferred from Direct Assay Assigned on 2009-02-23	Glover JR and Lindquist S  (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94(1):73-82	SGD
inheritance of oxidatively modified proteins involved in replicative cell aging	IGI: Inferred from Genetic Interaction with SGD:SIR2 Assigned on 2009-02-13 IMP: Inferred from Mutant Phenotype Assigned on 2009-02-13	Erjavec N, et al.  (2007) Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p. Genes Dev 21(19):2410-21	SGD
protein folding in endoplasmic reticulum	IMP: Inferred from Mutant Phenotype Assigned on 2009-02-13	Simola M, et al.  (2000) Trehalose is required for conformational repair of heat-denatured proteins in the yeast endoplasmic reticulum but not for maintenance of membrane traffic functions after severe heat stress. Mol Microbiol 37(1):42-53	SGD
protein unfolding	IMP: Inferred from Mutant Phenotype Assigned on 2009-02-13	Parsell DA, et al.  (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372(6505):475-8	SGD
trehalose metabolism in response to heat stress	IMP: Inferred from Mutant Phenotype Assigned on 2009-02-23	Iwahashi H, et al.  (1998) Evidence for the interplay between trehalose metabolism and Hsp104 in yeast. Appl Environ Microbiol 64(11):4614-7	SGD

Manually curated Cellular Component
Annotation(s)	Evidence	Reference(s)	Assigned By
cytoplasm	IDA: Inferred from Direct Assay Assigned on 2003-03-25	Kawai R, et al.  (1999) Direct evidence for the intracellular localization of Hsp104 in Saccharomyces cerevisiae by immunoelectron microscopy. Cell Stress Chaperones 4(1):46-53	SGD
nucleus	IDA: Inferred from Direct Assay Assigned on 2003-03-25	Kawai R, et al.  (1999) Direct evidence for the intracellular localization of Hsp104 in Saccharomyces cerevisiae by immunoelectron microscopy. Cell Stress Chaperones 4(1):46-53	SGD
TRC complex	IDA: Inferred from Direct Assay Assigned on 2010-12-01	Wang F, et al.  (2010) A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol Cell 40(1):159-71	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 2012-12-12	Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76	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:IPR013093, EBI:IPR003959, EBI:IPR001270, EBI:IPR018368 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
nucleoside-triphosphatase activity	IEA: Inferred from Electronic Annotation with EBI:IPR003593 Last updated 2013-03-02	DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms.	InterPro
nucleotide binding	IEA: Inferred from Electronic Annotation with EBI:IPR003593 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-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
protein metabolic process	IEA: Inferred from Electronic Annotation with EBI:IPR004176 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: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
nucleus	IEA: Inferred from Electronic Annotation with EBI:SL-0191 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-0539 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)).