# Hsp90 cochaperone STI1 YOR027W

> fungal protein found in Saccharomyces cerevisiae S288c

**Wikidata**: [Q27552181](https://www.wikidata.org/wiki/Q27552181)  
**Source**: https://4ort.xyz/entity/hsp90-cochaperone-sti1-yor027w


## References

1. UniProt
2. Q20641742
3. [InterPro Release 71.0](http://www.ebi.ac.uk/interpro/protein/P15705)
4. [A screen for RNA-binding proteins in yeast indicates dual functions for many enzymes.](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
5. [Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
6. [Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle](http://www.ebi.ac.uk/QuickGO/annotations?protein=P15705&geneProductId=UniProtKB:P15705)
7. [Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones](http://www.ebi.ac.uk/QuickGO/annotations?protein=P15705&geneProductId=UniProtKB:P15705)
8. [Sti1 Is a Novel Activator of the Ssa Proteins](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
9. [Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
10. [The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
11. [Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
12. [Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
13. [Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
14. [Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
15. [Proteome survey reveals modularity of the yeast cell machinery](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
16. [A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
17. [Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
18. [Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
19. [Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
20. [GOA](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
21. [In vivo analysis of the Hsp90 cochaperone Sti1 (p60)](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
22. [The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
23. [The cytosolic cochaperone Sti1 is relevant for mitochondrial biogenesis and morphology](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P15705)
24. ensembl Release 106