YEAST:HS104

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	HSP104
Protein Name(s)	Heat shock protein 104 Protein aggregation-remodeling factor HSP104
External Links
UniProt	P31539
EMBL	M67479 Z73131 Z73130 AY693002 X97560 BK006945
PIR	S61476
RefSeq	NP_013074.1
ProteinModelPortal	P31539
SMR	P31539
BioGrid	31226
DIP	DIP-2252N
IntAct	P31539
MINT	MINT-530773
STRING	4932.YLL026W
SWISS-2DPAGE	P31539
MaxQB	P31539
PaxDb	P31539
PeptideAtlas	P31539
EnsemblFungi	[example_ID YLL026W]
GeneID	850633
KEGG	sce:YLL026W
CYGD	YLL026w
SGD	S000003949
eggNOG	COG0542
GeneTree	ENSGT00390000012961
HOGENOM	HOG000218211
InParanoid	P31539
OMA	YINESEV
OrthoDB	EOG7X6M7K
BioCyc	YEAST:G3O-32130-MONOMER
SABIO-RK	P31539
NextBio	966553
PRO	PR:P31539
Proteomes	UP000002311
ExpressionAtlas	P31539
Genevestigator	P31539
GO	GO:0005737 GO:0005634 GO:0072380 GO:0043531 GO:0005524 GO:0042623 GO:0051087 GO:0051082 GO:0006200 GO:0070370 GO:0070389 GO:0001319 GO:0034975 GO:0043335 GO:0035617 GO:0070414
Gene3D	1.10.1780.10 3.40.50.300
InterPro	IPR003593 IPR003959 IPR019489 IPR004176 IPR001270 IPR018368 IPR028299 IPR023150 IPR027417
Pfam	PF00004 PF07724 PF02861 PF10431
PRINTS	PR00300
SMART	SM00382 SM01086
SUPFAM	SSF52540
PROSITE	PS00870 PS00871

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005737	cytoplasm		ECO:0000314			C		Source: SGD	Missing: reference
	GO:0005634	nucleus		ECO:0000314			C		Source: SGD	Missing: reference
	GO:0043531	ADP binding		ECO:0000315			F		Source: SGD	Missing: reference
	GO:0005524	ATP binding		ECO:0000315			F		Source: SGD	Missing: reference
	GO:0042623	ATPase activity, coupled		ECO:0000314			F		Source: SGD	Missing: reference
	GO:0051087	chaperone binding		ECO:0000314			F		Source: SGD	Missing: reference
	GO:0051082	unfolded protein binding		ECO:0000314			F		Source: SGD	Missing: reference
	GO:0070370	cellular heat acclimation		ECO:0000315			P		Source: SGD	Missing: reference
	GO:0070389	chaperone cofactor-dependent protein refolding		ECO:0000314			P		Source: SGD	Missing: reference
	GO:0001319	inheritance of oxidatively modified protein...		ECO:0000316			P		Source: SGD	Missing: with/from, reference
	GO:0034975	protein folding in endoplasmic reticulum		ECO:0000315			P		Source: SGD	Missing: reference
	GO:0043335	protein unfolding		ECO:0000315			P		Source: SGD	Missing: reference
	GO:0070414	trehalose metabolism in response to heat st...		ECO:0000315			P		Source: SGD	Missing: reference
part_of	GO:0005737	cytoplasm	PMID:22842922^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
	GO:0009408	response to heat	22579450:22579450	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 8983
part_of	GO:0034399	nuclear periphery	PMID:25817432^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0006974)	Seeded From UniProt	complete
involved_in	GO:0035617	stress granule disassembly	PMID:24291094^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	happens_during:(GO:0034605)	Seeded From UniProt	complete
part_of	GO:0072380	TRC complex	PMID:20850366^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0070414	trehalose metabolism in response to heat stress	PMID:9797333^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051085	chaperone cofactor-dependent protein refolding	PMID:9674429^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070370	cellular heat acclimation	PMID:2188365^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:9674429^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:16135516^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0043531	ADP binding	PMID:11867765^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0043335	protein unfolding	PMID:7984243^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042623	ATPase activity, coupled	PMID:9674429^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042623	ATPase activity, coupled	PMID:16135516^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042623	ATPase activity, coupled	PMID:16135516^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034975	protein folding in endoplasmic reticulum	PMID:10931304^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:10467108^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10467108^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:11867765^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0001319	inheritance of oxidatively modified proteins involved in replicative cell aging	PMID:17908928^[13]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000002200	P		Seeded From UniProt	complete
involved_in	GO:0001319	inheritance of oxidatively modified proteins involved in replicative cell aging	PMID:17908928^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21474779^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P31539	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20404203^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P31539	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:IPR001270 InterPro:IPR003959 InterPro:IPR018368	F		Seeded From UniProt	complete
involved_in	GO:0019538	protein metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR036628	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		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
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
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Notes

References

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

↑ Tkach, JM et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat. Cell Biol. 14 966-76 PubMed GONUTS page
↑ Gallina, I et al. (2015) Cmr1/WDR76 defines a nuclear genotoxic stress body linking genome integrity and protein quality control. Nat Commun 6 6533 PubMed GONUTS page
↑ Cherkasov, V et al. (2013) Coordination of translational control and protein homeostasis during severe heat stress. Curr. Biol. 23 2452-62 PubMed GONUTS page
↑ Wang, F et al. (2010) A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol. Cell 40 159-71 PubMed GONUTS page
↑ Iwahashi, H et al. (1998) Evidence for the interplay between trehalose metabolism and Hsp104 in yeast. Appl. Environ. Microbiol. 64 4614-7 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Glover, JR & Lindquist, S (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94 73-82 PubMed GONUTS page
↑ Sanchez, Y & Lindquist, SL (1990) HSP104 required for induced thermotolerance. Science 248 1112-5 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Bösl, B et al. (2005) Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides. J. Biol. Chem. 280 38170-6 PubMed GONUTS page
↑ ^9.0 ^9.1 Hattendorf, DA & 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 2732-7 PubMed GONUTS page
↑ Parsell, DA et al. (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372 475-8 PubMed GONUTS page
↑ 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 42-53 PubMed GONUTS page
↑ ^12.0 ^12.1 Kawai, R et al. (1999) Direct evidence for the intracellular localization of Hsp104 in Saccharomyces cerevisiae by immunoelectron microscopy. Cell Stress Chaperones 4 46-53 PubMed GONUTS page
↑ ^13.0 ^13.1 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 2410-21 PubMed GONUTS page
↑ Miot, M et al. (2011) Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. Proc. Natl. Acad. Sci. U.S.A. 108 6915-20 PubMed GONUTS page
↑ Lee, S et al. (2010) CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc. Natl. Acad. Sci. U.S.A. 107 8135-40 PubMed GONUTS page

[PMID:22842922-1] Tkach, JM et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat. Cell Biol. 14 966-76 PubMed GONUTS page

[PMID:25817432-2] Gallina, I et al. (2015) Cmr1/WDR76 defines a nuclear genotoxic stress body linking genome integrity and protein quality control. Nat Commun 6 6533 PubMed GONUTS page

[PMID:24291094-3] Cherkasov, V et al. (2013) Coordination of translational control and protein homeostasis during severe heat stress. Curr. Biol. 23 2452-62 PubMed GONUTS page

[PMID:20850366-4] Wang, F et al. (2010) A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol. Cell 40 159-71 PubMed GONUTS page

[PMID:9797333-5] Iwahashi, H et al. (1998) Evidence for the interplay between trehalose metabolism and Hsp104 in yeast. Appl. Environ. Microbiol. 64 4614-7 PubMed GONUTS page

[PMID:9674429-6] 6.0 ^6.1 ^6.2 Glover, JR & Lindquist, S (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94 73-82 PubMed GONUTS page

[PMID:2188365-7] Sanchez, Y & Lindquist, SL (1990) HSP104 required for induced thermotolerance. Science 248 1112-5 PubMed GONUTS page

[PMID:16135516-8] 8.0 ^8.1 ^8.2 Bösl, B et al. (2005) Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides. J. Biol. Chem. 280 38170-6 PubMed GONUTS page

[PMID:11867765-9] 9.0 ^9.1 Hattendorf, DA & 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 2732-7 PubMed GONUTS page

[PMID:7984243-10] Parsell, DA et al. (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372 475-8 PubMed GONUTS page

[PMID:10931304-11] 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 42-53 PubMed GONUTS page

[PMID:10467108-12] 12.0 ^12.1 Kawai, R et al. (1999) Direct evidence for the intracellular localization of Hsp104 in Saccharomyces cerevisiae by immunoelectron microscopy. Cell Stress Chaperones 4 46-53 PubMed GONUTS page

[PMID:17908928-13] 13.0 ^13.1 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 2410-21 PubMed GONUTS page

[PMID:21474779-14] Miot, M et al. (2011) Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. Proc. Natl. Acad. Sci. U.S.A. 108 6915-20 PubMed GONUTS page

[PMID:20404203-15] Lee, S et al. (2010) CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc. Natl. Acad. Sci. U.S.A. 107 8135-40 PubMed GONUTS page

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YEAST:HS104

Contents

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