YEAST:HSP82

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	HSP82 (synonyms: HSP90)
Protein Name(s)	ATP-dependent molecular chaperone HSP82 82 kDa heat shock protein Heat shock protein Hsp90 heat-inducible isoform
External Links
UniProt	P02829
EMBL	K01387 Z67751 Z73596 BK006949
PIR	A03313
RefSeq	NP_015084.1
PDB	1A4H 1AH6 1AH8 1AM1 1AMW 1BGQ 1HK7 1US7 1USU 1USV 1ZW9 1ZWH 2AKP 2BRC 2BRE 2CG9 2CGE 2CGF 2FXS 2IWS 2IWU 2IWX 2LSV 2VW5 2VWC 2WEP 2WEQ 2WER 2XD6 2XX2 2XX4 2XX5 2YGA 2YGE 2YGF 3C0E 3C11 3FP2 4AS9 4ASA 4ASB 4ASF 4ASG 4CE1 4CE2 4CE3
PDBsum	1A4H 1AH6 1AH8 1AM1 1AMW 1BGQ 1HK7 1US7 1USU 1USV 1ZW9 1ZWH 2AKP 2BRC 2BRE 2CG9 2CGE 2CGF 2FXS 2IWS 2IWU 2IWX 2LSV 2VW5 2VWC 2WEP 2WEQ 2WER 2XD6 2XX2 2XX4 2XX5 2YGA 2YGE 2YGF 3C0E 3C11 3FP2 4AS9 4ASA 4ASB 4ASF 4ASG 4CE1 4CE2 4CE3
ProteinModelPortal	P02829
SMR	P02829
BioGrid	35923
DIP	DIP-2262N
IntAct	P02829
MINT	MINT-560200
STRING	4932.YPL240C
BindingDB	P02829
ChEMBL	CHEMBL3536
SWISS-2DPAGE	P02829
MaxQB	P02829
PeptideAtlas	P02829
PRIDE	P02829
EnsemblFungi	[example_ID YPL240C]
GeneID	855836
KEGG	sce:YPL240C
CYGD	YPL240c
SGD	S000006161
GeneTree	ENSGT00770000120625
HOGENOM	HOG000031988
InParanoid	P02829
KO	K04079
OMA	ITRMHEI
OrthoDB	EOG7BP8B5
BioCyc	YEAST:G3O-34126-MONOMER
Reactome	REACT_189032 REACT_189238 REACT_209789 REACT_219346
EvolutionaryTrace	P02829
NextBio	980407
Proteomes	UP000002311
Genevestigator	P02829
GO	GO:0005737 GO:0005524 GO:0042623 GO:0042802 GO:0051082 GO:0006458 GO:0006200 GO:0000492 GO:0032212 GO:0043248 GO:0042026 GO:0006626 GO:0006970
Gene3D	3.30.565.10
HAMAP	MF_00505
InterPro	IPR003594 IPR019805 IPR001404 IPR020575 IPR020568
PANTHER	PTHR11528
Pfam	PF02518 PF00183
PIRSF	PIRSF002583
PRINTS	PR00775
SMART	SM00387
SUPFAM	SSF54211 SSF55874
PROSITE	PS00298

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0032204	regulation of telomere maintenance	PMID:21829731^[1]	ECO:0000315			P	Figure 1B.	complete CACAO 1992
	GO:0009408	response to heat	PMID:22579450^[2]	ECO:0000314			P	Figure 3 represents assays on the amount of the protein present after heat was applied. Expression was measured using RNeasy Mini Kit. Selected primers were seen in table 1	complete CACAO 8982
part_of	GO:0005737	cytoplasm	PMID:11914276^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:14562095^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0051604	protein maturation	PMID:27068472^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042623	ATPase activity, coupled	PMID:27068472^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:27385335^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0032204	regulation of telomere maintenance	PMID:21829731^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:10564510^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0043248	proteasome assembly	PMID:12853471^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043248	proteasome assembly	PMID:12853471^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042623	ATPase activity, coupled	PMID:12235160^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	PMID:9371781^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032212	positive regulation of telomere maintenance via telomerase	PMID:17954556^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032212	positive regulation of telomere maintenance via telomerase	PMID:17954556^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006970	response to osmotic stress	PMID:16487343^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006626	protein targeting to mitochondrion	PMID:12526792^[13]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000005065	P	Seeded From UniProt	complete
involved_in	GO:0006458	'de novo' protein folding	PMID:9371781^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006458	'de novo' protein folding	PMID:10564510^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000492	box C/D snoRNP assembly	PMID:18268103^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0001233 PANTHER:PTN000163629 PomBase:SPAC926.04c SGD:S000004798 SGD:S000006161	F	Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000163629 UniProtKB:P07900 UniProtKB:P11501	P	Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0001233 MGI:MGI:96250 PANTHER:PTN000163629 RGD:631409 WB:WBGene00000915	C	Seeded From UniProt	complete
enables	GO:0042623	ATPase activity, coupled	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 PANTHER:PTN000898156 SGD:S000006161	F	Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 PANTHER:PTN000163629 SGD:S000004798	P	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000163629 RGD:631409 UniProtKB:P07900 UniProtKB:P11501 WB:WBGene00000915	C	Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 PANTHER:PTN000163629 RGD:631409 UniProtKB:P11501	C	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 FB:FBgn0001233 PANTHER:PTN000163629 RGD:631409 SGD:S000004798 UniProtKB:P11501	P	Seeded From UniProt	complete
part_of	GO:0009277	fungal-type cell wall	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 PANTHER:PTN000898156 UniProtKB:P40292	C	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 MGI:MGI:96250 PANTHER:PTN000163629 RGD:631409 TAIR:locus:2161775 TAIR:locus:2161790 UniProtKB:P11501	C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96250 PANTHER:PTN000163629 RGD:631409 TAIR:locus:2161775 UniProtKB:P11501 UniProtKB:P40292 dictyBase:DDB_G0267400	C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000201062 FB:FBgn0001233 MGI:MGI:96250 PANTHER:PTN000163629 RGD:631409 SGD:S000006161 TAIR:locus:2161775 TAIR:locus:2161790 UniProtKB:P07900 UniProtKB:P11501 UniProtKB:P40292 UniProtKB:Q76LV2 UniProtKB:Q8I0V4 WB:WBGene00000915 ZFIN:ZDB-GENE-990415-94 dictyBase:DDB_G0267400	C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000898156 PomBase:SPAC926.04c	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24794838^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02829	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23396352^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02829	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20736353^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02829	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19696785^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02829	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18268103^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02829	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16625188^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02829	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001404 InterPro:IPR019805	F	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001404 InterPro:IPR019805	P	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001404 InterPro:IPR019805	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Laskar, S et al. (2011) HSP90 controls SIR2 mediated gene silencing. PLoS ONE 6 e23406 PubMed GONUTS page
↑ Auesukaree, C et al. (2012) Characterization and gene expression profiles of thermotolerant Saccharomyces cerevisiae isolates from Thai fruits. J. Biosci. Bioeng. 114 144-9 PubMed GONUTS page
↑ Kumar, A et al. (2002) Subcellular localization of the yeast proteome. Genes Dev. 16 707-19 PubMed GONUTS page
↑ Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page
↑ ^5.0 ^5.1 Mishra, P et al. (2016) Systematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 Function. Cell Rep 15 588-598 PubMed GONUTS page
↑ Finnigan, GC et al. (2016) Detection of protein-protein interactions at the septin collar in Saccharomyces cerevisiae using a tripartite split-GFP system. Mol. Biol. Cell 27 2708-25 PubMed GONUTS page
↑ ^7.0 ^7.1 Scheibel, T et al. (1999) Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae. Mol. Microbiol. 34 701-13 PubMed GONUTS page
↑ ^8.0 ^8.1 Imai, J et al. (2003) The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J. 22 3557-67 PubMed GONUTS page
↑ Richter, K et al. (2002) N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle. J. Biol. Chem. 277 44905-10 PubMed GONUTS page
↑ ^10.0 ^10.1 Nathan, DF et al. (1997) In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc. Natl. Acad. Sci. U.S.A. 94 12949-56 PubMed GONUTS page
↑ ^11.0 ^11.1 Toogun, OA et al. (2008) The hsp90 molecular chaperone modulates multiple telomerase activities. Mol. Cell. Biol. 28 457-67 PubMed GONUTS page
↑ Yang, XX et al. (2006) The molecular chaperone Hsp90 is required for high osmotic stress response in Saccharomyces cerevisiae. FEMS Yeast Res. 6 195-204 PubMed GONUTS page
↑ Young, JC et al. (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112 41-50 PubMed GONUTS page
↑ ^14.0 ^14.1 Zhao, R et al. (2008) Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J. Cell Biol. 180 563-78 PubMed GONUTS page
↑ ^15.00 ^15.01 ^15.02 ^15.03 ^15.04 ^15.05 ^15.06 ^15.07 ^15.08 ^15.09 ^15.10 ^15.11 ^15.12 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Pal, M et al. (2014) Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure 22 805-18 PubMed GONUTS page
↑ Li, J et al. (2013) Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Nat. Struct. Mol. Biol. 20 326-31 PubMed GONUTS page
↑ Ratzke, C et al. (2010) Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle. Proc. Natl. Acad. Sci. U.S.A. 107 16101-6 PubMed GONUTS page
↑ Retzlaff, M et al. (2009) Hsp90 is regulated by a switch point in the C-terminal domain. EMBO Rep. 10 1147-53 PubMed GONUTS page
↑ Ali, MM et al. (2006) Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440 1013-7 PubMed GONUTS page

[PMID:21829731-1] 1.0 ^1.1 Laskar, S et al. (2011) HSP90 controls SIR2 mediated gene silencing. PLoS ONE 6 e23406 PubMed GONUTS page

[PMID:22579450-2] Auesukaree, C et al. (2012) Characterization and gene expression profiles of thermotolerant Saccharomyces cerevisiae isolates from Thai fruits. J. Biosci. Bioeng. 114 144-9 PubMed GONUTS page

[PMID:11914276-3] Kumar, A et al. (2002) Subcellular localization of the yeast proteome. Genes Dev. 16 707-19 PubMed GONUTS page

[PMID:14562095-4] Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page

[PMID:27068472-5] 5.0 ^5.1 Mishra, P et al. (2016) Systematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 Function. Cell Rep 15 588-598 PubMed GONUTS page

[PMID:27385335-6] Finnigan, GC et al. (2016) Detection of protein-protein interactions at the septin collar in Saccharomyces cerevisiae using a tripartite split-GFP system. Mol. Biol. Cell 27 2708-25 PubMed GONUTS page

[PMID:10564510-7] 7.0 ^7.1 Scheibel, T et al. (1999) Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae. Mol. Microbiol. 34 701-13 PubMed GONUTS page

[PMID:12853471-8] 8.0 ^8.1 Imai, J et al. (2003) The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J. 22 3557-67 PubMed GONUTS page

[PMID:12235160-9] Richter, K et al. (2002) N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle. J. Biol. Chem. 277 44905-10 PubMed GONUTS page

[PMID:9371781-10] 10.0 ^10.1 Nathan, DF et al. (1997) In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc. Natl. Acad. Sci. U.S.A. 94 12949-56 PubMed GONUTS page

[PMID:17954556-11] 11.0 ^11.1 Toogun, OA et al. (2008) The hsp90 molecular chaperone modulates multiple telomerase activities. Mol. Cell. Biol. 28 457-67 PubMed GONUTS page

[PMID:16487343-12] Yang, XX et al. (2006) The molecular chaperone Hsp90 is required for high osmotic stress response in Saccharomyces cerevisiae. FEMS Yeast Res. 6 195-204 PubMed GONUTS page

[PMID:12526792-13] Young, JC et al. (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112 41-50 PubMed GONUTS page

[PMID:18268103-14] 14.0 ^14.1 Zhao, R et al. (2008) Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J. Cell Biol. 180 563-78 PubMed GONUTS page

[PMID:21873635-15] 15.00 ^15.01 ^15.02 ^15.03 ^15.04 ^15.05 ^15.06 ^15.07 ^15.08 ^15.09 ^15.10 ^15.11 ^15.12 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:24794838-16] Pal, M et al. (2014) Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure 22 805-18 PubMed GONUTS page

[PMID:23396352-17] Li, J et al. (2013) Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Nat. Struct. Mol. Biol. 20 326-31 PubMed GONUTS page

[PMID:20736353-18] Ratzke, C et al. (2010) Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle. Proc. Natl. Acad. Sci. U.S.A. 107 16101-6 PubMed GONUTS page

[PMID:19696785-19] Retzlaff, M et al. (2009) Hsp90 is regulated by a switch point in the C-terminal domain. EMBO Rep. 10 1147-53 PubMed GONUTS page

[PMID:16625188-20] Ali, MM et al. (2006) Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440 1013-7 PubMed GONUTS page

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YEAST:HSP82

Contents

Annotations

Notes

References

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