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YEAST:HSP26

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) HSP26
Protein Name(s) Heat shock protein 26

26 kDa heat shock protein

External Links
UniProt P15992
EMBL M23871
M26942
X76294
Z35941
AY692975
BK006936
PIR S45465
RefSeq NP_009628.1
ProteinModelPortal P15992
SMR P15992
BioGrid 32775
DIP DIP-3988N
IntAct P15992
MINT MINT-536537
STRING 4932.YBR072W
MaxQB P15992
PaxDb P15992
PeptideAtlas P15992
EnsemblFungi [example_ID YBR072W]
GeneID 852364
KEGG sce:YBR072W
SGD S000000276
eggNOG COG0071
HOGENOM HOG000112974
InParanoid P15992
KO K13993
OMA KLEPREN
OrthoDB EOG7B5X7W
BioCyc YEAST:G3O-29041-MONOMER
NextBio 971137
Proteomes UP000002311
Genevestigator P15992
GO GO:0005737
GO:0010494
GO:0005634
GO:0003729
GO:0051082
GO:0034605
GO:0006457
Gene3D 2.60.40.790
InterPro IPR002068
IPR008978
Pfam PF00011
SUPFAM SSF49764
PROSITE PS01031

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0005739

mitochondrion

PMID:24769239[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

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 8981

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:0010494

cytoplasmic stress granule

PMID:26777405[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0010494

cytoplasmic stress granule

PMID:24291094[5]

ECO:0000314

direct assay evidence used in manual assertion

C

part_of:(GO:0034605)

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:10581247[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:10581247[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:10581247[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:2645298[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:2645298[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003729

mRNA binding

PMID:20844764[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18719252[9]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P15992

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16843901[10]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P15992

F

Seeded From UniProt

complete

Notes

References

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

  1. Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 PubMed GONUTS page
  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
  3. Kumar, A et al. (2002) Subcellular localization of the yeast proteome. Genes Dev. 16 707-19 PubMed GONUTS page
  4. Jain, S et al. (2016) ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure. Cell 164 487-98 PubMed GONUTS page
  5. Cherkasov, V et al. (2013) Coordination of translational control and protein homeostasis during severe heat stress. Curr. Biol. 23 2452-62 PubMed GONUTS page
  6. 6.0 6.1 6.2 Haslbeck, M et al. (1999) Hsp26: a temperature-regulated chaperone. EMBO J. 18 6744-51 PubMed GONUTS page
  7. 7.0 7.1 Rossi, JM & Lindquist, S (1989) The intracellular location of yeast heat-shock protein 26 varies with metabolism. J. Cell Biol. 108 425-39 PubMed GONUTS page
  8. Tsvetanova, NG et al. (2010) Proteome-wide search reveals unexpected RNA-binding proteins in Saccharomyces cerevisiae. PLoS ONE 5 PubMed GONUTS page
  9. Yu, H et al. (2008) High-quality binary protein interaction map of the yeast interactome network. Science 322 104-10 PubMed GONUTS page
  10. White, HE et al. (2006) Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Structure 14 1197-204 PubMed GONUTS page